Vet Med - Czech, 2012, 57(9):439-513 | DOI: 10.17221/6336-VETMED

Single-domain antibody fragments derived from heavy-chain antibodies: a review

L. Eyer, K. Hruska
Veterinary Research Institute, Brno, Czech Republic

Single-domain antibody (sdAb) fragments derived from heavy-chain antibodies of camelids and cartilaginous fish represent a new generation of therapeutic agents and immunoreagents. Due to their unique characteristics, such as low molecular weight, high physical-chemical stability, good water solubility, and the ability to bind antigens inaccessible to conventional antibodies, they could potentially act as a substitute for conventional therapeutic drugs in the treatment of serious human diseases, and, moreover, could be broadly used in analyses and diagnostics. In this review article, an analysis of 826 publications oriented to heavy-chain antibodies and their sdAb fragments indexed in the Web of Science® database since 1993 has been carried out. Attention has predominantly been paid to papers published from 2010 to June 2012. Key publications are presented in tables and are characterised by descriptive words, abstracts and references. The presented publications have been sorted according to seven basic criteria: review articles and monographs, heavy-chain antibodies of camelids and sharks, production of sdAb fragments using recombinant technology, characteristic properties of sdAb fragments, application of sdAb fragments in therapy, application of sdAb fragments in diagnostic and immunoanalytical methods and other prospective uses of sdAb fragments. This review article should highlight the typical properties of heavy-chain antibodies and sdAb fragments which differentiate them from conventional antibodies and other available recombinant fragments, and also emphasize their extremely broad application potential, mainly in human disease therapy. At the same time it allows an easy and rapid orientation in numerous publications written on this subject, and facilitates the search for the required data.

Keywords: single-domain antibody fragment; heavy-chain antibody; antigen-binding site; camelid; shark; therapy; recombinant technology

Published: September 30, 2012  Show citation

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Eyer L, Hruska K. Single-domain antibody fragments derived from heavy-chain antibodies: a review. Vet Med - Czech. 2012;57(9):439-513. doi: 10.17221/6336-VETMED.
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References

  1. Abskharon RNN, Soror SH, Pardon E, El Hassan H, Legname G, Steyaert J, Wohlkonig A (2011): Combining in-situ proteolysis and microseed matrix screening to promote crystallization of PrP(c)-nanobody complexes. Protein Engineering Design and Selection 24, 737-741. Go to original source... Go to PubMed...
  2. Abulrob A, Sprong H, Henegouwen PVBE, Stanimirovic D (2005): The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells. Journal of Neurochemistry 95, 1201-1214. Go to original source... Go to PubMed...
  3. Aladin F, Einerhand AWC, Bouma J, Bezemer S, Hermans P, Wolvers D, Bellamy K, Frenken LGJ, Gray J, Iturriza-Gomara M (2012): In vitro neutralisation of rotavirus infection by two broadly specific recombinant monovalent llama-derived antibody fragments. Plos One 7. Go to original source...
  4. Altintas I, Kok RJ, Schiffelers RM (2012): Targeting epidermal growth factor receptor in tumors: From conventional monoclonal antibodies via heavy chainonly antibodies to nanobodies. European Journal of Pharmaceutical Sciences 45, 399-407. Go to original source... Go to PubMed...
  5. Alvarez-Rueda N, Behar G, Ferre V, Pugniere M, Roquet F, Gastinel L, Jacquot C, Aubry J, Baty D, Barbet J, Birkle S (2007): Generation of llama single-domain antibodies against methotrexate, a prototypical hapten. Molecular Immunology 44, 1680-1690. Go to original source... Go to PubMed...
  6. Alzogaray V, Danquah W, Aguirre A, Urrutia M, Berguer P, Vescovi EG, Haag F, Koch-Nolte F, Goldbaum FA (2011): Single-domain llama antibodies as specific intracellular inhibitors of SpvB, the actin ADP-ribosylating toxin of Salmonella typhimurium. Faseb Journal 25, 526-534. Go to original source... Go to PubMed...
  7. Anderson GP, Bernstein RD, Swain MD, Zabetakis D, Goldman ER (2010): Binding kinetics of antiricin single domain antibodies and improved detection using a B chain specific binder. Analytical Chemistry 82, 7202-7207. Go to original source... Go to PubMed...
  8. Anderson GP, Goldman ER (2008): TNT detection using llama antibodies and a two-step competitive fluid array immunoassay. Journal of Immunological Methods 339, 47-54. Go to original source... Go to PubMed...
  9. Baral TN, Magez S, Stijlemans B, Conrath K, Vanhollebeke B, Pays E, Muyldermans S, De Baetselier P (2006): Experimental therapy of African trypanosomiasis with a nanobody-conjugated human trypanolytic factor. Nature Medicine 12, 580-584. Go to original source... Go to PubMed...
  10. Baral TN, Murad Y, Nguyen TD, Iqbal U, Zhang JB (2011): Isolation of functional single domain antibody by whole cell immunization: Implications for cancer treatment. Journal of Immunological Methods 371, 70-80. Go to original source... Go to PubMed...
  11. Bazl MR, Rasaee MJ, Foruzandeh M, Rahimpour A, Kiani J, Rahbarizadeh F, Alirezapour B, Mohammadi M (2007): Production of chimeric recombinant single domain antibody-green fluorescent fusion protein in Chinese hamster ovary cells. Hybridoma 26, 1-9. Go to original source... Go to PubMed...
  12. Behdani M, Zeinali S, Khanahmad H, Karimipour M, Asadzadeh N, Azadmanesh K, Khabiri A, Schoonooghe S, Anbouhi MH, Hassanzadeh-Ghassabeh G, Muyldermans S (2012): Generation and characterization of a functional Nanobody against the vascular endothelial growth factor receptor-2; angiogenesis cell receptor. Molecular Immunology 50, 35-41. Go to original source... Go to PubMed...
  13. Bell A, Wang ZJ, Arbabi-Ghahroudi M, Chang TTA, Durocher Y, Trojahn U, Baardsnes J, Jaramillo ML, Li SH, Baral TN, O'Connor-McCourt M, MacKenzie R, Zhang JB (2010): Differential tumor-targeting abilities of three single-domain antibody formats. Cancer Letters 289, 81-90. Go to original source... Go to PubMed...
  14. Ben Abderrazek R, Vincke C, Hmila I, Saerens D, Abidi N, El Ayeb M, Muyldermans S, Bouhaouala-Zahar B (2011): Development of Cys38 knock-out and humanized version of NbAahII10 nanobody with improved neutralization of AahII Scorpion toxin. Protein Engineering Design and Selection 24, 727-735. Go to original source... Go to PubMed...
  15. Blanco-Toribio A, Muyldermans S, Frankel G, Fernandez LA (2010): Direct injection of functional single-domain antibodies from E. coli into human cells. Plos One 5. Go to original source...
  16. Broisat A, Hernot S, Toczek J, De Vos J, Riou LM, Martin S, Ahmadi M, Thielens N, Wernery U, Caveliers V, Muyldermans S, Lahoutte T, Fagret D, Ghezzi C, Devoogdt N (2012): Nanobodies targeting mouse/human VCAM1 for the nuclear imaging of atherosclerotic lesions. Circulation Research 110, 927-937. Go to original source... Go to PubMed...
  17. Caljon G, Caveliers V, Lahoutte T, Stijlemans B, Ghassabeh GH, Van Den Abbeele J, Smolders I, De Baetselier P, Michotte Y, Muyldermans S, Magez S, Clinckers R (2012): Using microdialysis to analyse the passage of monovalent nanobodies through the blood-brain barrier. British Journal of Pharmacology 165, 2341-2353. Go to original source... Go to PubMed...
  18. Caussinus E, Kanca O, Affolter M (2012): Fluorescent fusion protein knockout mediated by anti-GFP nanobody. Nature Structural and Molecular Biology 19, 117-121. Go to original source... Go to PubMed...
  19. Conrad U, Plagmann I, Malchow S, Sack M, Floss DM, Kruglov AA, Nedospasov SA, Rose-John S, Scheller J (2011): ELPylated anti-human TNF therapeutic singledomain antibodies for prevention of lethal septic shock. Plant Biotechnology Journal 9, 22-31. Go to original source... Go to PubMed...
  20. Conrath KE, Wernery U, Muyldermans S, Nguyen VK (2003): Emergence and evolution of functional heavychain antibodies in Camelidae. Developmental and Comparative Immunology 27, 87-103. Go to original source... Go to PubMed...
  21. Conrath K, Vincke C, Stijlemans B, Schymkowitz J, Decanniere K, Wyns L, Muyldermans S, Loris R (2005): Antigen binding and solubility effects upon veneering of a camel VHH in framework-2 to the mimic a VH. Journal of Molecular Biology 350, 112-125. Go to original source... Go to PubMed...
  22. Conway JO, Sherwood LJ, Collazo MT, Garza JA, Hayhurst A (2010): Llama single domain antibodies specific for the 7 botulinum neurotoxin serotypes as heptaplex immunoreagents. Plos One 5. Go to original source...
  23. Cortez-Retamozo V, Lauwereys M, Gh GH, Gobert M, Conrath K, Muyldermans S, De Baetselier P, Revets H (2002): Efficient tumor targeting by single-domain antibody fragments of camels. International Journal of Cancer 98, 456-462. Go to original source... Go to PubMed...
  24. Cortez-Retamozo V, Backmann N, Senter PD, Wernery U, De Baetselier P, Muyldermans S, Revets H (2004): Efficient cancer therapy with a nanobody-based conjugate. Cancer Research 64, 2853-2857. Go to original source... Go to PubMed...
  25. Daley LP, Kutzler MA, Bennett BW, Smith MC, Glaser AL, Appleton JA (2010): Effector functions of camelid heavy-chain antibodies in immunity to West Nile virus. Clinical and Vaccine Immunology 17, 239-246. Go to original source... Go to PubMed...
  26. De Genst E, Silence K, Decanniere K, Conrath K, Loris R, Kinne R, Muyldermans S, Wyns L (2006): Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. Proceedings of the National Academy of Sciences of the United States of America 103, 4586-4591. Go to original source... Go to PubMed...
  27. De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, Meehan S, Dumoulin M, Hsu STD, Cremades N, Verschueren KHG, Pardon E, Wyns L, Steyaert J, Christodoulou J, Dobson CM (2010): Structure and properties of a complex of alpha-synuclein and a single-domain camelid antibody. Journal of Molecular Biology 402, 326-343. Go to original source... Go to PubMed...
  28. de Marco A (2011): Biotechnological applications of recombinant single-domain antibody fragments. Microbial Cell Factories 10, 44. Go to original source... Go to PubMed...
  29. De Marni ML, Monegal A, Venturini S, Vinati S, Carbone R, de Marco A (2012): Antibody purification-independent microarrays (PIM) by direct bacteria spotting on TiO2-treated slides. Methods 56, 317-325. Go to original source... Go to PubMed...
  30. De Vooght L, Caljon G, Stijlemans B, De Baetselier P, Coosemans M, Van Den Abbeele J (2012): Expression and extracellular release of a functional anti-trypanosome Nanobody (R) in Sodalis glossinidius, a bacterial symbiont of the tsetse fly. Microbial Cell Factories 11, 23. Go to original source... Go to PubMed...
  31. Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, Wyns L (1999): A single-domain antibody fragment in complex with RNase A: noncanonical loop structures and nanomolar affinity using two CDR loops. Structure with Folding and Design 7, 361-370. Go to original source... Go to PubMed...
  32. Deckers N, Saerens D, Kanobana K, Conrath K, Victor B, Wernery U, Vercruysse J, Muyldermans S, Dorny P (2009): Nanobodies, a promising tool for speciesspecific diagnosis of Taenia solium cysticercosis. International Journal for Parasitology 39, 625-633. Go to original source... Go to PubMed...
  33. Deffar K, Shi HL, Li L, Wang XZ, Zhu XJ (2009): Nanobodies - the new concept in antibody engineering. African Journal of Biotechnology 8, 2645-2652.
  34. Delanote V, Vanloo B, Catillon M, Friederich E, Vandekerckhove J, Gettemans J (2010): An alpaca singledomain antibody blocks filopodia formation by obstructing L-plastin-mediated F-actin bundling. Faseb Journal 24, 105-118. Go to original source... Go to PubMed...
  35. Dolk E, van der Vaart M, Hulsik DL, Vriend G, de Haard H, Spinelli S, Cambillau C, Frenken L, Verrips T (2005a): Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. Applied and Environmental Microbiology 71, 442-450. Go to original source... Go to PubMed...
  36. Dolk E, van Vliet C, Perez JMJ, Vriend G, Darbon H, Ferrat G, Cambillau C, Frenken LGJ, Verrips T (2005b): Induced refolding of a temperature denatured llama heavy-chain antibody fragment by its antigen. Proteins-Structure Function and Bioinformatics 59, 555- 564. Go to original source... Go to PubMed...
  37. Domanska K, Vanderhaegen S, Srinivasan V, Pardon E, Dupeux F, Marquez JA, Giorgetti S, Stoppini M, Wyns L, Bellotti V, Steyaert J (2011): Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta 2-microglobulin variant. Proceedings of the National Academy of Sciences of the United States of America 108, 1314-1319. Go to original source... Go to PubMed...
  38. Dona V, Urrutia M, Bayardo M, Alzogaray V, Goldbaum FA, Chirdo FG (2010): Single domain antibodies are specially suited for quantitative determination of gliadins under denaturing conditions. Journal of Agricultural and Food Chemistry 58, 918-926. Go to original source... Go to PubMed...
  39. Dumoulin M, Conrath K, Van Meirhaeghe A, Meersman F, Heremans K, Frenken LGJ, Muyldermans S, Wyns L, Matagne A (2002): Single-domain antibody fragments with high conformational stability. Protein Science 11, 500-515. Go to original source... Go to PubMed...
  40. Emmerson CD, van der Vlist EJ, Braam MR, Vanlandschoot P, Merchiers P, de Haard HJW, Verrips CT, Henegouwen PMPV, Dolk E (2011): Enhancement of polymeric immunoglobulin receptor transcytosis by biparatopic VHH. Plos One 6. Go to original source...
  41. Ezzine A, el Adab SM, Bouhaouala-Zahar B, Hmila I, Baciou L, Marzouki MN (2012): Efficient expression of the anti-AahI' scorpion toxin nanobody under a new functional form in a Pichia pastoris system. Biotechnology and Applied Biochemistry 59, 15-21. Go to original source... Go to PubMed...
  42. Fanning SW, Horn JR (2011): An anti-hapten camelid antibody reveals a cryptic binding site with significant energetic contributions from a nonhypervariable loop. Protein Science 20, 1196-1207. Go to original source... Go to PubMed...
  43. Fennell BJ, Darmanin-Sheehan A, Hufton SE, Calabro V, Wu L, Muller MR, Cao W, Gill D, Cunningham O, Finlay WJJ (2010): Dissection of the IgNAR V domain: Molecular scanning and orthologue database mining define novel IgNAR hallmarks and affinity maturation mechanisms. Journal of Molecular Biology 400, 155-170. Go to original source... Go to PubMed...
  44. Ferrari A, Rodriguez MM, Power P, Weill FS, De Simone EA, Gutkind G, Leoni J (2007): Immunobiological role of llama heavy-chain antibodies against a bacterial beta-lactamase. Veterinary Immunology and Immunopathology 117, 173-182. Go to original source... Go to PubMed...
  45. Flajnik MF, Deschacht N, Muyldermans S (2011): A case of convergence: Why did a simple alternative to canonical antibodies arise in sharks and camels? Plos Biology 9. Go to original source... Go to PubMed...
  46. Forsman A, Beirnaert E, Aasa-Chapman MMI, Hoorelbeke B, Hijazi K, Koh W, Tack V, Szynol A, Kelly C, McKnight A, Verrips T, de Haard H, Weiss RA (2008): Llama antibody fragments with cross-subtype human immunodeficiency virus Type 1 (HIV-1)-neutralizing properties and high affinity for HIV-1 gp120. Journal of Virology 82, 12069-12081. Go to original source... Go to PubMed...
  47. Franco EJ, Sonneson GJ, DeLegge TJ, Hofstetter H, Horn JR, Hofstetter O (2010): Production and characterization of a genetically engineered anti-caffeine camelid antibody and its use in immunoaffinity chromatography. Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences 878, 177-186. Go to original source... Go to PubMed...
  48. Gainkam LOT, Keyaerts M, Caveliers V, Devoogdt N, Vanhove C, Van Grunsven L, Muyldermans S, Lahoutte T (2011): Correlation between epidermal growth factor receptor-specific nanobody uptake and burden: A tool for noninvasive monitoring of tumor response to therapy. Molecular Imaging and Biology 13, 940-948. Go to original source... Go to PubMed...
  49. Goldman ER, Anderson GP, Bernstein RD, Swain MD (2010): Amplification of immunoassays using phagedisplayed single domain antibodies. Journal of Immunological Methods 352, 182-185. Go to original source... Go to PubMed...
  50. Goodchild SA, Dooley H, Schoepp RJ, Flajnik M, Lonsdale SG (2011): Isolation and characterisation of Ebolavirus-specific recombinant antibody fragments from murine and shark immune libraries. Molecular Immunology 48, 2027-2037. Go to original source... Go to PubMed...
  51. Gorlani A, Hulsik DL, Adams H, Vriend G, Hermans P, Verrips T (2012): Antibody engineering reveals the important role of J segments in the production efficiency of llama single-domain antibodies in Saccharomyces cerevisiae. Protein Engineering Design and Selection 25, 39-46. Go to original source... Go to PubMed...
  52. Govaert J, Pellis M, Deschacht N, Vincke C, Conrath K, Muyldermans S, Saerens D (2012): Dual beneficial effect of interloop disulfide bond for single domain antibody fragments. Journal of Biological Chemistry 287, 1970-1979. Go to original source... Go to PubMed...
  53. Graef RR, Anderson GP, Doyle KA, Zabetakis D, Sutton FN, Liu JL, Serrano-Gonzalez J, Goldman ER, Cooper LA (2011): Isolation of a highly thermal stable lama single domain antibody specific for Staphylococcus aureus Enterotoxin B. BMC Biotechnology 11. Go to original source... Go to PubMed...
  54. Greenberg AS, Avila D, Hughes M, Hughes A, Mckinney EC, Flajnik MF (1995): A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature 374, 168-173. Go to original source... Go to PubMed...
  55. Hamerscasterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N, Hamers R (1993): Naturally-occurring antibodies devoid of light-chains. Nature 363, 446-448. Go to original source... Go to PubMed...
  56. Harmsen MM, de Haard HJ (2007): Properties, production, and applications of camelid single-domain antibody fragments. Applied Microbiology and Biotechnology 77, 13-22. Go to original source... Go to PubMed...
  57. Harmsen MM, van Solt CB, Fijten HPD, Van Setten MC (2005): Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins. Vaccine 23, 4926-4934. Go to original source... Go to PubMed...
  58. Harmsen MM, van Solt CB, van Bemmel AMV, Niewold TA, van Zijderveld FG (2006): Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy. Applied Microbiology and Biotechnology 72, 544-551. Go to original source... Go to PubMed...
  59. Henderson KA, Streltsov VA, Coley AM, Dolezal O, Hudson PJ, Batchelor AH, Gupta A, Bai T, Murphy VJ, Anders RF, Foley M, Nuttall SD (2007): Structure of an IgNAR-AMA1 complex: Targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure 15, 1452-1466. Go to original source... Go to PubMed...
  60. Hendrickx MLV, De Winter A, Buelens K, Compernolle G, Hassanzadeh-Ghassabeh G, Muyldermans S, Gils A, Declerck PJ (2011): TAFIa inhibiting nanobodies as profibrinolytic tools and discovery of a new TAFIa conformation. Journal of Thrombosis and Haemostasis 9, 2268-2277. Go to original source... Go to PubMed...
  61. Holliger P, Hudson PJ (2005): Engineered antibody fragments and the rise of single domains. Nature Biotechnology 23, 1126-1136. Go to original source... Go to PubMed...
  62. Honda Y, Kondo H, Caipang CMA, Hirono I, Aoki T (2010): cDNA cloning of the immunoglobulin heavy chain genes in banded houndshark Triakis scyllium. Fish and Shellfish Immunology 29, 854-861. Go to original source... Go to PubMed...
  63. Huang L, Muyldermans S, Saerens D (2010): Nanobodies (R): proficient tools in diagnostics. Expert Review of Molecular Diagnostics 10, 777-785. Go to original source... Go to PubMed...
  64. Hultberg A, Tremblay DM, de Haard H, Verrips T, Moineau S, Hammarstom L, Marcotte H (2007): Lactobacillli expressing llama VHH fragments neutralise Lactococcus phages. BMC Biotechnology 7, 58. Go to original source... Go to PubMed...
  65. Hultberg A, Temperton NJ, Rosseels V, Koenders M, Gonzalez-Pajuelo M, Schepens B, Ibanez LI, Vanlandschoot P, Schillemans J, Saunders M, Weiss RA, Saelens X, Melero JA, Verrips CT, Van Gucht S, de Haard HJ (2011): Llama-derived single domain antibodies to build multivalent, superpotent and broadened neutralizing anti-viral molecules. Plos One 6. Go to original source...
  66. Hussack G, Luo Y, Veldhuis L, Hall JC, Tanha J, MacKenzie R (2009): Multivalent anchoring and oriented display of single-domain antibodies on cellulose. Sensors 9, 5351-5367. Go to original source... Go to PubMed...
  67. Hussack G, Hirama T, Ding W, MacKenzie R, Tanha J (2011a): Engineered single-domain antibodies with high protease resistance and thermal stability. Plos One 6. Go to original source...
  68. Hussack G, Arbabi-Ghahroudi M, van Faassen H, Songer JG, Ng KKS, MacKenzie R, Tanha J (2011b): Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain. Journal of Biological Chemistry 286, 8961-8976. Go to original source... Go to PubMed...
  69. Ibanez LI, De Filette M, Hultberg A, Verrips T, Temperton N, Weiss RA, Vandevelde W, Schepens B, Vanlandschoot P, Saelens X (2011): Nanobodies with in vitro neutralizing activity protect mice against H5N1 influenza virus infection. Journal of Infectious Diseases 203, 1063-1072. Go to original source... Go to PubMed...
  70. Impagliazzo A, Tepper AW, Verrips TC, Ubbink M, van der Maarel SM (2010): Structural basis for a PABPN1 aggregation-preventing antibody fragment in OPMD. Febs Letters 584, 1558-1564. Go to original source... Go to PubMed...
  71. Inoue H, Ilhara A, Takahashi H, Shimada I, Ishida I, Maeda Y (2011): Affinity transfer to a human protein by CDR3 grafting of camelid VHH. Protein Science 20, 1971-1981. Go to original source... Go to PubMed...
  72. Iqbal U, Abulrob A, Stanimirovic DB (2011): Integrated platform for brain imaging and drug delivery across the blood-brain barrier. Blood-Brain and Other Neural Barriers: Reviews and Protocols 686, 465-481. Go to original source... Go to PubMed...
  73. Iri-Sofla FJ, Rahbarizadeh F, Ahmadvand D, Rasaee MJ (2011): Nanobody-based chimeric receptor gene integration in Jurkat cells mediated by PhiC31 integrase. Experimental Cell Research 317, 2630-2641. Go to original source... Go to PubMed...
  74. Jahnichen S, Blanchetot C, Maussang D, Gonzalez-Pajuelo M, Chow KY, Bosch L, De Vrieze S, Serruys B, Ulrichts H, Vandevelde W, Saunders M, de Haard HJ, Schols D, Leurs R, Vanlandschoot P, Verrips T, Smit MJ (2010): CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells. Proceedings of the National Academy of Sciences of the United States of America 107, 20565-20570. Go to original source... Go to PubMed...
  75. Jamnani FR, Rahbarizadeh F, Shokrgozar MA, Ahmadvand D, Mahboudi F, Sharifzadeh Z (2012): Targeting high affinity and epitope-distinct oligoclonal nanobodies to HER2 over-expressing tumor cells. Experimental Cell Research 318, 1112-1124. Go to original source... Go to PubMed...
  76. Joosten V, Gouka RJ, van den Hondel CAMJ, Verrips CT, Lokman BC (2005): Expression and production of llama variable heavy-chain antibody fragments (V(HH)s) by Aspergillus awamori. Applied Microbiology and Biotechnology 66, 384-392. Go to original source... Go to PubMed...
  77. Kasturirangan S, Boddapati S, Sierks MR (2010): Engineered proteolytic nanobodies reduce A beta burden and ameliorate A beta-induced cytotoxicity. Biochemistry 49, 4501-4508. Go to original source... Go to PubMed...
  78. Kim HJ, Mccoy MR, Majkova Z, Dechant JE, Gee SJ, Tabares-da Rosa S, Gonzalez-Sapienza GG, Hammock BD (2012): Isolation of alpaca anti-hapten heavy chain single domain antibodies for development of sensitive immunoassay. Analytical Chemistry 84, 1165-1171. Go to original source... Go to PubMed...
  79. Kirchhofer A, Helma J, Schmidthals K, Frauer C, Cui S, Karcher A, Pellis M, Muyldermans S, Casas-Delucchi CS, Cardoso MC, Leonhardt H, Hopfner KP, Rothbauer U (2010): Modulation of protein properties in living cells using nanobodies. Nature Structural and Molecular Biology 17, 133-138. Go to original source... Go to PubMed...
  80. Koide S (2009): Engineering of recombinant crystallization chaperones. Current Opinion in Structural Biology 19, 449-457. Go to original source... Go to PubMed...
  81. Korouzhdehy B, Dadmehr M, Piri I, Rahbarizadeh F, Solouki M (2011): Expression of biological active VHH camelid single domain antibody in transgenic tobacco. African Journal of Biotechnology 10, 4234-4241.
  82. Ladenson RC, Crimmins DL, Landt Y, Ladenson JH (2006): Isolation and characterization of a thermally stable recombinant anti-caffeine heavy-chain antibody fragment. Analytical Chemistry 78, 4501-4508. Go to original source... Go to PubMed...
  83. Lafaye P, Achour I, England P, Duyckaerts C, Rougeon F (2009): Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent A beta-induced neurotoxicity and inhibit fibril formation. Molecular Immunology 46, 695-704. Go to original source... Go to PubMed...
  84. Lauwereys M, Ghahroudi MA, Desmyter A, Kinne J, Holzer W, De Genst E, Wyns L, Muyldermans S (1998): Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. Embo Journal 17, 3512-3520. Go to original source... Go to PubMed...
  85. Li JW, Xia LJ, Su YH, Liu HC, Xia XQ, Lu QX, Yang CJ, Reheman K (2012): Molecular imprint of enzyme active site by camel nanobodies rapid and efficient approach to produce abzymes with alliinase activity. Journal of Biological Chemistry 287, 13713-13721. Go to original source... Go to PubMed...
  86. Makvandi-Nejad S, Fjallman T, Arbabi-Ghahroudi M, MacKenzie CR, Hall JC (2011): Selection and expression of recombinant single domain antibodies from a hyper-immunized library against the hapten azoxystrobin. Journal of Immunological Methods 373, 8-18. Go to original source... Go to PubMed...
  87. Martin MC, Pant N, Ladero V, Gunaydin G, Andersen KK, Alvarez B, Martinez N, Alvarez MA, Hammarstrom L, Marcotte H (2011): Integrative expression system for delivery of antibody fragments by Lactobacilli. Applied and Environmental Microbiology 77, 2174-2179. Go to original source... Go to PubMed...
  88. McGonigal K, Tanha J, Palazov E, Li SH, GueorguievaOwens D, Pandey S (2009): Isolation and functional characterization of single domain antibody modulators of caspase-3 and apoptosis. Applied Biochemistry and Biotechnology 157, 226-236. Go to original source... Go to PubMed...
  89. Moller A, Pion E, Narayan V, Ball KL (2010): Intracellular activation of interferon regulatory factor-1 by nanobodies to the multifunctional (Mf1) domain. Journal of Biological Chemistry 285, 38348-38361. Go to original source... Go to PubMed...
  90. Murtaugh ML, Fanning SW, Sharma TM, Terry AM, Horn JR (2011): A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches. Protein Science 20, 1619-1631. Go to original source... Go to PubMed...
  91. Muyldermans S, Cambillau C, Wyns L (2001): Recognition of antigens by single domain antibody fragments: the superfluous luxury of paired domains. Trends in Biochemical Sciences 26, 230-235. Go to original source... Go to PubMed...
  92. Muyldermans S, Baral TN, Retarnozzo VC, De Baetselier P, De Genst E, Kinne J, Leonhardt H, Magez S, Nguyen VK, Revets H, Rothbauer U, Stijemans B, Tillib S, Wernery U, Wyns L, Hassanzadeh-Ghassabeh G, Saerens D (2009): Camelid immunoglobulins and nanobody technology. Veterinary Immunology and Immunopathology 128, 178-183. Go to original source... Go to PubMed...
  93. Nguyen VK, Hamers R, Wyns L, Muyldermans S (1999): Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies. Molecular Immunology 36, 515-524. Go to original source... Go to PubMed...
  94. Nguyen VK, Hamers R, Wyns L, Muyldermans S (2000): Camel heavy-chain antibodies: diverse germline VHH and specific mechanisms enlarge the antigen-binding repertoire. EMBO Journal 19, 921-930. Go to original source... Go to PubMed...
  95. Nguyen VK, Su C, Muyldermans S, van der Loo W (2002): Heavy-chain antibodies in Camelidae; a case of evolutionary innovation. Immunogenetics 54, 39-47. Go to original source... Go to PubMed...
  96. Oliveira S, Schiffelers RM, van der Veeken J, van der Meel R, Vongpromek R, Henegouwen PMPV, Storm G, Roovers RC (2010): Downregulation of EGFR by a novel multivalent nanobody-liposome platform. Journal of Controlled Release 145, 165-175. Go to original source... Go to PubMed...
  97. Omidfar K, Rasaee MJ, Kashanian S, Paknejad M, Bathaie Z (2007): Studies of thermostability in Camelus bactrianus (Bactrian camel) single-domain antibody specific for the mutant epidermal-growth-factor receptor expressed by Pichia. Biotechnology and Applied Biochemistry 46, 41-49. Go to original source... Go to PubMed...
  98. Oyen D, Srinivasan V, Steyaert J, Barlow JN (2011): Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition. Journal of Molecular Biology 407, 138-148. Go to original source... Go to PubMed...
  99. Paalanen MMI, Ekokoski E, El Khattabi M, Tuominen RK, Verrips CT, Boonstra J, Blanchetot C (2011): The development of activating and inhibiting camelid VHH domains against human protein kinase C epsilon. European Journal of Pharmaceutical Sciences 42, 332-339. Go to original source... Go to PubMed...
  100. Pant N, Hultberg A, Zhao YF, Svensson L, Pan-Hammarstrom Q, Johansen K, Pouwels PH, Ruggeri FM, Hermans P, Frenken L, Boren T, Marcotte H, Hammarstrom L (2006): Lactobacilli expressing variable domain of llama heavy-chain antibody fragments (lactobodies) confer protection against rotavirus-induced diarrhea. Journal of Infectious Diseases 194, 1580-1588. Go to original source... Go to PubMed...
  101. Park YJ, Pardon E, Wu MT, Steyaert J, Hol WGJ (2012): Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody. Nucleic Acids Research 40, 1828-1840. Go to original source... Go to PubMed...
  102. Pollithy A, Romer T, Lang C, Muller FD, Helma J, Leonhardt H, Rothbauer U, Schuler D (2011): Magnetosome expression of functional camelid antibody fragments (nanobodies) in Magnetospirillum gryphiswaldense. Applied and Environmental Microbiology 77, 6165-6171. Go to original source... Go to PubMed...
  103. Pooja J, Ajit S (2010): Staphylococcus aureus beta-hemolysin-neutralizing single-domain antibody isolated from phage display library of Indian desert camel. Asian Pacific Journal of Tropical Medicine 3, 1-7. Go to original source...
  104. Ratier L, Urrutia M, Paris G, Zarebski L, Frasch AC, Goldbaum FA (2008): Relevance of the diversity among members of the Trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies. Plos One 3. Go to original source...
  105. Resemann A, Wunderlich D, Rothbauer U, Warscheid B, Leonhardt H, Fuchser J, Kuhlmann K, Suckau D (2010): Top-down de novo protein sequencing of a 13.6 kDa came lid single heavy chain antibody by matrix-assisted laser desorption ionization-time-offlight/time-of-flight mass spectrometry. Analytical Chemistry 82, 3283-3292. Go to original source... Go to PubMed...
  106. Reyelt J, Schwarz N, Haag F, Goldbaum F, Koch-Nolte F (2006): Manipulating the signaling functions of extracellular NAD with recombinant 'nanobodies' that block the active site of a leucocyte cell surface ectoenzyme. Molecular Medicine 12, S21-S22.
  107. Romer T, Leonhardt H, Rothbauer U (2011): Engineering antibodies and proteins for molecular in vivo imaging. Current Opinion in Biotechnology 22, 882-887. Go to original source... Go to PubMed...
  108. Roovers RC, van Dongen GAMS, Henegouwen PMPV (2007): Nanobodies in therapeutic applications. Current Opinion in Molecular Therapeutics 9, 327-335. Go to PubMed...
  109. Roovers RC, Vosjan MJWD, Laeremans T, el Khoulati R, de Bruin RCG, Ferguson KM, Verkleij AJ, van Dongen GAMS, Henegouwen PMPV (2011): A biparatopic antiEGFR nanobody efficiently inhibits solid tumour growth. International Journal of Cancer 129, 2013-2024. Go to original source... Go to PubMed...
  110. Rutgers KS, Nabuurs RJA, van den Berg SAA, Schenk GJ, Rotman M, Verrips CT, van Duinen SG, MaatSchieman ML, van Buchem MA, de Boer AG, van der Maarel SM (2011): Transmigration of beta amyloid specific heavy chain antibody fragments across the in vitro blood-brain barrier. Neuroscience 190, 37-42. Go to original source... Go to PubMed...
  111. Ryckaert S, Pardon E, Steyaert J, Callewaert N (2010): Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. Journal of Biotechnology 145, 93-98. Go to original source... Go to PubMed...
  112. Saccodossi N, De Simone EA, Leoni J (2012): Structural analysis of effector functions related motifs, complement activation and hemagglutinating activities in Lama glama heavy chain antibodies. Veterinary Immunology and Immunopathology 145, 323-331. Go to original source... Go to PubMed...
  113. Saerens D, Muyldermans S (eds.) (2012): Single Domain Antibodies. Springer, New York. 580 pp. http://www.springer.com/biomed/immunology/book/978-1-61779-967-9 Go to original source...
  114. Saerens D, Pellis M, Loris R, Pardon E, Dumoulin M, Matagne A, Wyns L, Muyldermans S, Conrath K (2005): Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies. Journal of Molecular Biology 352, 597-607. Go to original source... Go to PubMed...
  115. Saerens D, Ghassabeh GH, Muyldermans S (2008): Single-domain antibodies as building blocks for novel therapeutics. Current Opinion in Pharmacology 8, 600-608. Go to original source... Go to PubMed...
  116. Schmidthals K, Helma J, Zolghadr K, Rothbauer U, Leonhardt H (2010): Novel antibody derivatives for proteome and high-content analysis. Analytical and Bioanalytical Chemistry 397, 3203-3208. Go to original source... Go to PubMed...
  117. Serruys B, Van Houtte F, Farhoudi-Moghadam A, Leroux-Roels G, Vanlandschoot P (2010): Production, characterization and in vitro testing of HBcAg-specific VHH intrabodies. Journal of General Virology 91, 643-652. Go to original source... Go to PubMed...
  118. Simmons DP, Streltsov VA, Dolezal O, Hudson PJ, Coley AM, Foley M, Proll DF, Nuttall SD (2008): Shark IgNAR antibody mimotopes target a murine immunoglobulin through extended CDR3 loop structures. Proteins-Structure Function and Bioinformatics 71, 119-130. Go to original source... Go to PubMed...
  119. Sircar A, Sanni KA, Shi JY, Gray JJ (2011): Analysis and modeling of the variable region of camelid single-domain antibodies. Journal of Immunology 186, 6357-6367. Go to original source... Go to PubMed...
  120. Smith LE, Crouch K, Cao W, Muller MR, Wu LY, Steven J, Lee M, Liang MS, Flajnik MF, Shih HH, Barelle CJ, Paulsen J, Gill DS, Dooley H (2012): Characterization of the immunoglobulin repertoire of the spiny dogfish (Squalus acanthias). Developmental and Comparative Immunology 36, 665-679. Go to original source... Go to PubMed...
  121. Smolarek D, Hattab C, Hassanzadeh-Ghassabeh G, Cochet S, Gutierrez C, de Brevern AG, Udomsangpetch R, Picot J, Grodecka M, Wasniowska K, Muyldermans S, Colin Y, Le Van Kim C, Czerwinski M, Bertrand O (2010): A recombinant dromedary antibody fragment (VHH or nanobody) directed against human Duffy antigen receptor for chemokines. Cellular and Molecular Life Sciences 67, 3371-3387. Go to original source... Go to PubMed...
  122. Spinelli S, Tegoni M, Frenken L, van Vliet C, Cambillau C (2001): Lateral recognition of a dye hapten by a llama VHH domain. Journal of Molecular Biology 311, 123- 129. Go to original source... Go to PubMed...
  123. Stijlemans B, Conrath K, Cortez-Retamozo V, Van Xong H, Wyns L, Senter P, Revets H, De Baetselier P, Muyldermans S, Magez S (2004): Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies - African trypanosomes as paradigm. Journal of Biological Chemistry 279, 1256-1261. Go to original source... Go to PubMed...
  124. Stijlemans B, Caljon G, Natesan SKA, Saerens D, Conrath K, Perez-Morga D, Skepper JN, Nikolaou A, Brys L, Pays E, Magez S, Field MC, De Baetselier P, Muyldermans S (2011): High affinity nanobodies against the Trypanosome brucei VSG are potent trypanolytic agents that block endocytosis. Plos Pathogens 7. Go to original source... Go to PubMed...
  125. Stone E, Hirama T, Tanha J, Tong-Sevinc H, Li SH, MacKenzie CR, Zhang JB (2007): The assembly of single domain antibodies into bispecific decavalent molecules. Journal of Immunological Methods 318, 88-94. Go to original source... Go to PubMed...
  126. Streltsov VA, Carmichael JA, Nuttall SD (2005): Structure of a shark IgNAR antibody variable domain and modeling of an early-developmental isotype. Protein Science 14, 2901-2909. Go to original source... Go to PubMed...
  127. Strokappe N, Szynol A, Aasa-Chapman M, Gorlani A, Quigley AF, Hulsik DL, Chen L, Weiss R, de Haard H, Verrips T (2012): Llama Antibody Fragments Recognizing Various Epitopes of the CD4bs Neutralize a Broad Range of HIV-1 Subtypes A, B and C. Plos One 7. Go to original source...
  128. Sukhanova A, Even-Desrumeaux K, Kisserli A, Tabary T, Reveil B, Millot JM, Chames P, Baty D, Artemyev M, Oleinikov V, Pluot M, Cohen JHM, Nabiev I (2012): Oriented conjugates of single-domain antibodies and quantum dots: toward a new generation of ultrasmall diagnostic nanoprobes. Nanomedicine-Nanotechnology Biology and Medicine 8, 516-525. Go to original source... Go to PubMed...
  129. Swain MD, Anderson GP, Zabetakis D, Bernstein RD, Liu JL, Sherwood LJ, Hayhurst A, Goldman ER (2010): Llama-derived single-domain antibodies for the detection of botulinum A neurotoxin. Analytical and Bioanalytical Chemistry 398, 339-348. Go to original source... Go to PubMed...
  130. Swain MD, Anderson GP, Serrano-Gonzalez J, Liu JL, Zabetakis D, Goldman ER (2011): Immunodiagnostic reagents using llama single domain antibody-alkaline phosphatase fusion proteins. Analytical Biochemistry 417, 188-194. Go to original source... Go to PubMed...
  131. Szynol A, de Soet JJ, Sieben-van Tuyl E, Bos JW, Frenken LG (2004): Bactericidal effects of a fusion protein of llama heavy-chain antibodies coupled to glucose oxidase on oral bacteria. Antimicrobial Agents and Chemotherapy 48, 3390-3395. Go to original source... Go to PubMed...
  132. Tabares-da Rosa S, Rossotti M, Carleiza C, Carrion F, Pritsch O, Ahn KC, Last JA, Hammock BD, GonzalezSapienza G (2011): Competitive selection from single domain antibody libraries allows isolation of high-affinity antihapten antibodies that are not favored in the llama immune response. Analytical Chemistry 83, 7213-7220. Go to original source... Go to PubMed...
  133. Talelli M, Iman M, Rijcken CJF, van Nostrum CF, Hennink WE (2010): Targeted core-crosslinked polymeric micelles with controlled release of covalently entrapped doxorubicin. Journal of Controlled Release 148, E121- E122. Go to original source... Go to PubMed...
  134. Talelli M, Rijcken CJF, Oliveira S, van der Meel R, Henegouwen PMPV, Lammers T, van Nostrum CF, Storm G, Hennink WE (2011): Nanobody - shell functionalized thermosensitive core-crosslinked polymeric micelles for active drug targeting. Journal of Controlled Release 151, 183-192. Go to original source... Go to PubMed...
  135. Tayebi M, Taylor WA, Jones DR, Bate C, David M (2010): PrP-specific camel antibodies with the ability to immunodetect intracellular prion protein. Journal of General Virology 91, 2121-2131. Go to original source... Go to PubMed...
  136. Teh YHA, Kavanagh TA (2010): High-level expression of camelid nanobodies in Nicotiana benthamiana. Transgenic Research 19, 575-586. Go to original source... Go to PubMed...
  137. Tillib SV (2011): "Camel nanoantibody"is an efficient tool for research, diagnostics and therapy. Molecular Biology 45, 66-73. Go to original source...
  138. Torigoe T, Asanuma H, Nakazawa E, Tamura Y, Hirohashi Y, Yamamoto E, Kanaseki T, Hasegawa T, Sato N (2012): Establishment of a monoclonal anti-pan HLA class I antibody suitable for immunostaining of formalin-fixed tissue: Unusually high frequency of down-regulation in breast cancer tissues. Pathology International 62, 303-308. Go to original source... Go to PubMed...
  139. Tremblay JM, Kuo CL, Abeijon C, Sepulveda J, Oyler G, Hu XB, Jin MM, Shoemaker CB (2010): Camelid single domain antibodies (VHHs) as neuronal cell intrabody binding agents and inhibitors of Clostridium botulinum neurotoxin (BoNT) proteases. Toxicon 56, 990-998. Go to original source... Go to PubMed...
  140. Trilling AK, de Ronde H, Noteboom L, van Houwelingen A, Roelse M, Srivastava SK, Haasnoot W, Jongsma MA, Kolk A, Zuilhof H, Beekwilder J (2011): A broad set of different llama antibodies specific for a 16 kDa heat shock protein of Mycobacterium tuberculosis. Plos One 6. Go to original source... Go to PubMed...
  141. Udata C, Mukherjee A, Hutmacher M, Peterson M, Liao KH, Checchio T, Shields K, Meng X, Comer G (2011): Pharmacokinetic-pharmacodynamic modeling of ozoralizumab (ATN-103), a novel humanized nanobody tumor necrosis factor inhibitor for rheumatoid arthritis. Arthritis and Rheumatism 63, S493.
  142. Van Bockstaele F, Holz JB, Revets H (2009): The development of nanobodies for therapeutic applications. Current Opinion in Investigational Drugs 10, 1212-1224.
  143. Van de Broek B, Devoogdt N, D'Hollander A, Gijs HL, Jans K, Lagae L, Muyldermans S, Maes G, Borghs G (2011): Specific cell targeting with nanobody conjugated branched gold nanoparticles for photothermal therapy. ACS Nano 5, 4319-4328. Go to original source... Go to PubMed...
  144. Vandenbroucke K, de Haard H, Beirnaert E, Dreier T, Lauwereys M, Huyck L, Van Huysse J, Demetter P, Steidler L, Remaut E, Cuvelier C, Rottiers P (2010): Orally administered L. lactis secreting an anti-TNF Nanobody demonstrate efficacy in chronic colitis. Mucosal Immunology 3, 49-56. Go to original source... Go to PubMed...
  145. Vaneycken I, Govaert J, Vincke C, Caveliers V, Lahoutte T, De Baetselier P, Raes G, Bossuyt A, Muyldermans S, Devoogdt N (2010): In vitro analysis and in vivo tumor targeting of a humanized, grafted nanobody in mice using Pinhole SPECT/Micro-CT. Journal of Nuclear Medicine 51, 1099-1106. Go to original source... Go to PubMed...
  146. Vaneycken I, D'Huyvetter M, Hernot S, De Vos J, Xavier C, Devoogdt N, Caveliers V, Lahoutte T (2011a): Immuno-imaging using nanobodies. Current Opinion in Biotechnology 22, 877-881. Go to original source... Go to PubMed...
  147. Vaneycken I, Devoogdt N, Van Gassen N, Vincke C, Xavier C, Wernery U, Muyldermans S, Lahoutte T, Caveliers V (2011b): Preclinical screening of anti-HER2 nanobodies for molecular imaging of breast cancer. FASEB Journal 25, 2433-2446. Go to original source... Go to PubMed...
  148. Vanlandschoot P, Stortelers C, Beirnaert E, Ibanez LI, Schepens B, Depla E, Saelens X (2011): Nanobodies (R): New ammunition to battle viruses. Antiviral Research 92, 389-407. Go to original source... Go to PubMed...
  149. Veggiani G, de Marco A (2011): Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidase. Protein Expression and Purification 79, 111-114. Go to original source... Go to PubMed...
  150. Vercruysse T, Pardon E, Vanstreels E, Steyaert J, Daelemans D (2010): An intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 Rev prevents viral production. Journal of Biological Chemistry 285, 21768-21780. Go to original source... Go to PubMed...
  151. Vincke C, Loris R, Saerens D, Martinez-Rodriguez S, Muyldermans S, Conrath K (2009): General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold. Journal of Biological Chemistry 284, 3273-3284. Go to original source... Go to PubMed...
  152. Vuchelen A, O'Day E, De Genst E, Pardon E, Wyns L, Dumoulin M, Dobson CM, Christodoulou J, Hsu STD (2009): H-1, C-13 and N-15 assignments of a camelid nanobody directed against human alpha-synuclein. Biomolecular NMR Assignments 3, 231-233. Go to original source... Go to PubMed...
  153. Walper SA, Anderson GP, Lee PAB, Glaven RH, Liu JL, Bernstein RD, Zabetakis D, Johnson L, Czarnecki JM, Goldman ER (2012): Rugged single domain antibody detection elements for Bacillus anthracis spores and vegetative Cells. Plos One 7. Go to original source...
  154. Walsh R, Nuttall S, Revill P, Colledge D, Cabuang L, Soppe S, Dolezal O, Griffiths K, Bartholomeusz A, Locarnini S (2011): Targeting the hepatitis B virus precore antigen with a novel IgNAR single variable domain intrabody. Virology 411, 132-141. Go to original source... Go to PubMed...
  155. Wei GW, Meng WX, Guo HJ, Pan WQ, Liu JS, Peng T, Chen L, Chen CY (2011): Potent neutralization of influenza A virus by a single-domain antibody blocking M2 ion channel protein. Plos One 6. Go to original source...
  156. Wernery U (2001): Camelid immunoglobulins and their importance for the new-born - A review. Journal of Veterinary Medicine Series B-Infectious Diseases and Veterinary Public Health 48, 561-568. Go to original source... Go to PubMed...
  157. Wesolowski J, Alzogaray V, Reyelt J, Unger M, Juarez K, Urrutia M, Cauerhff A, Danquah W, Rissiek B, Scheuplein F, Schwarz N, Adriouch S, Boyer O, Seman M, Licea A, Serreze DV, Goldbaum FA, Haag F, KochNolte F (2009): Single domain antibodies: promising experimental and therapeutic tools in infection and immunity. Medical Microbiology and Immunology 198, 157-174. Go to original source... Go to PubMed...
  158. Yau KYF, Groves MAT, Li SH, Sheedy C, Lee H, Tanha J, MacKenzie CR, Jermutus L, Hall JC (2003): Selection of hapten-specific single-domain antibodies from a non-immunized llama ribosome display library. Journal of Immunological Methods 281, 161-175. Go to original source... Go to PubMed...
  159. Zabeau L, Verhee A, Catteeuw D, Faes L, Seeuws S, Decruy T, Elewaut D, Peelman F, Tavernier J (2012): Selection of non-competitive leptin antagonists using a random nanobody-based approach. Biochemical Journal 441, 425-434. Go to original source... Go to PubMed...
  160. Zhang JB, Tanha J, Hirama T, Khieu NH, To R, Hong TS, Stone E, Brisson JR, MacKenzie CR (2004): Pentamerization of single-domain antibodies from phage libraries: A novel strategy for the rapid generation of high-avidity antibody reagents. Journal of Molecular Biology 335, 49-56. Go to original source... Go to PubMed...
  161. Zou XG, Smith JA, Nguyen VK, Ren LM, Luyten K, Muyldermans S, Bruggemann M (2005): Expression of a dromedary heavy chain-only antibody and B cell development in the mouse. Journal of Immunology 175, 3769-3779. Go to original source... Go to PubMed...

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