Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs)

Journal of Immunological Methods

Volumn 324, Issue 1-2, 2007, Pages 13-25

  Maass, David R ^a   Sepulveda, Jorge ^c   Pernthaner, Anton ^b   Shoemaker, Charles B ^c  

^a VICTORIA UNIVERSITY OF WELLINGTON   (New Zealand)

^b AGRESEARCH GRASSLANDS   (New Zealand)

^c TUFTS UNIVERSITY   (United States)

Author keywords

Alpaca; Camelid; HCAb; Recombinant antibody; TNF; VHH

Indexed keywords

HEAVY CHAIN IMMUNOGLOBULIN G; IMMUNOGLOBULIN G ANTIBODY; RECOMBINANT ANTIBODY; RECOMBINANT CAMELID HEAVY CHAIN ANTIBODY; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VHH ANTIBODY;

AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ANTIBODY ISOLATION; ANTIBODY PRODUCTION; ANTIGEN BINDING; ARTICLE; CAMEL; CONTROLLED STUDY; DNA LIBRARY; DNA SEQUENCE; GENETIC CODE; IMMUNOGENETICS; LAMA PACOS; LYMPH NODE; MALE; NONHUMAN; PHAGE DISPLAY; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; UNGULATE;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CAMELIDS, NEW WORLD; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MALE; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SHEEP;

CAMELIDAE; LAMA GLAMA; LAMA PACOS; OVIS;

EID: 34347248421     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2007.04.008     Document Type: Article

References (37)

1. Abuzakouk M., Feighery C., and Jackson J. Tumour necrosis factor blocking agents: a new therapeutic modality for inflammatory disorders. Br. J. Biomed. Sci. 59 (2002) 173
2. Arbabi Ghahroudi M., Desmyter A., Wyns L., Hamers R., and Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 414 (1997) 521
3. Basalp A., and Yucel F. Development of mouse hybridomas by fusion of myeloma cells with lymphocytes derived from spleen, lymph node, and bone marrow. Hybrid Hybridomics 22 (2003) 329
4. Daley L.P., Gagliardo L.F., Duffy M.S., Smith M.C., and Appleton J.A. Application of monoclonal antibodies in functional and comparative investigations of heavy-chain immunoglobulins in new world camelids. Clin. Diagn. Lab. Immunol. 12 (2005) 380
5. De Genst E., Saerens D., Muyldermans S., and Conrath K. Antibody repertoire development in camelids. Dev Comp Immunol 30 (2006) 187
6. Decanniere K., Muyldermans S., and Wyns L. Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?. J Mol Biol 300 (2000) 83
7. Dumoulin M., Conrath K., Van Meirhaeghe A., Meersman F., Heremans K., Frenken L.G., Muyldermans S., Wyns L., and Matagne A. Single-domain antibody fragments with high conformational stability. Protein Sci 11 (2002) 500
8. Flick D.A., and Gifford G.E. Comparison of in vitro cell cytotoxic assays for tumor necrosis factor. J Immunol Methods 68 (1984) 167
9. Frenken L.G., van der Linden R.H., Hermans P.W., Bos J.W., Ruuls R.C., de Geus B., and Verrips C.T. Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J Biotechnol 78 (2000) 11
10. Friguet B., Djavadi-Ohaniance L., Pages J., Bussard A., and Goldberg M. A convenient enzyme-linked immunosorbent assay for testing whether monoclonal antibodies recognize the same antigenic site. Application to hybridomas specific for the beta 2-subunit of Escherichia coli tryptophan synthase. J Immunol Methods 60 (1983) 351
11. Gibbs W.W. Nanobodies. Sci Am 293 (2005) 78
12. Green R.S., Douch P.G., Hill F.I., Death A.F., Wyeth T.K., and Donaghy M.J. Antibody responses of grazing alpacas (Lama pacos) in New Zealand to intestinal nematodes. Int J Parasitol 26 (1996) 429
13. Guzman L.M., Belin D., Carson M.J., and Beckwith J. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177 (1995) 4121
14. Hamers-Casterman C., Atarhouch T., Muyldermans S., Robinson G., Hamers C., Songa E.B., Bendahman N., and Hamers R. Naturally occurring antibodies devoid of light chains. Nature 363 (1993) 446
15. Harmsen M.M., Ruuls R.C., Nijman I.J., Niewold T.A., Frenken L.G., and de Geus B. Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features. Mol Immunol 37 (2000) 579
16. Lauwereys M., Arbabi Ghahroudi M., Desmyter A., Kinne J., Holzer W., De Genst E., Wyns L., and Muyldermans S. Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. Embo J 17 (1998) 3512
17. Lawrence C.E., Paterson J.C., Higgins L.M., MacDonald T.T., Kennedy M.W., and Garside P. IL-4-regulated enteropathy in an intestinal nematode infection. Eur J Immunol 28 (1998) 2672
18. Lefranc M.P., Giudicelli V., Ginestoux C., Bodmer J., Muller W., Bontrop R., Lemaitre M., Malik A., Barbie V., and Chaume D. IMGT, the international ImMunoGeneTics database. Nucleic Acids Res 27 (1999) 209
19. Lefranc M.P., Pommie C., Kaas Q., Duprat E., Bosc N., Guiraudou D., Jean C., Ruiz M., Da Piedade I., Rouard M., Foulquier E., Thouvenin V., and Lefranc G. IMGT unique numbering for immunoglobulin and T cell receptor constant domains and Ig superfamily C-like domains. Dev Comp Immunol 29 (2005) 185
20. Li F., and Aitken R. Cloning of porcine scFv antibodies by phage display and expression in Escherichia coli. Vet Immunol Immunopathol 97 (2004) 39
21. Liesenfeld O., Kang H., Park D., Nguyen T.A., Parkhe C.V., Watanabe H., Abo T., Sher A., Remington J.S., and Suzuki Y. TNF-alpha, nitric oxide and IFN-gamma are all critical for development of necrosis in the small intestine and early mortality in genetically susceptible mice infected perorally with Toxoplasma gondii. Parasite Immunol 21 (1999) 365
22. Marini M., Bamias G., Rivera-Nieves J., Moskaluk C.A., Hoang S.B., Ross W.G., Pizarro T.T., and Cominelli F. TNF-alpha neutralization ameliorates the severity of murine Crohn's-like ileitis by abrogation of intestinal epithelial cell apoptosis. Proc Natl Acad Sci U S A 100 (2003) 8366
23. Muyldermans S., Atarhouch T., Saldanha J., Barbosa J.A., and Hamers R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng 7 (1994) 1129
24. Nash A.D., Barcham G.J., Brandon M.R., and Andrews A.E. Molecular cloning, expression and characterization of ovine TNF alpha. Immunol Cell Biol 69 Pt 4 (1991) 273
25. Nguyen V.K., Desmyter A., and Muyldermans S. Functional heavy-chain antibodies in Camelidae. Adv Immunol 79 (2001) 261
26. Nguyen V.K., Hamers R., Wyns L., and Muyldermans S. 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. Mol Immunol 36 (1999) 515
27. Pernthaner A., Cole S.A., Morrison L., and Hein W.R. Increased expression of interleukin-5 (IL-5), IL-13, and tumor necrosis factor alpha genes in intestinal lymph cells of sheep selected for enhanced resistance to nematodes during infection with Trichostrongylus colubriformis. Infect Immun 73 (2005) 2175
28. Rothbauer U., Zolghadr K., Tillib S., Nowak D., Schermelleh L., Gahl A., Backmann N., Conrath K., Muyldermans S., Cardoso M.C., and Leonhardt H. Targeting and tracing antigens in live cells with fluorescent nanobodies. Nat Methods 3 (2006) 887
29. Ruuls S.R., and Sedgwick J.D. Unlinking tumor necrosis factor biology from the major histocompatibility complex: lessons from human genetics and animal models. Am J Hum Genet 65 (1999) 294
30. Saerens D., Kinne J., Bosmans E., Wernery U., Muyldermans S., and Conrath K. Single domain antibodies derived from dromedary lymph node and peripheral blood lymphocytes sensing conformational variants of prostate-specific antigen. J Biol Chem 279 (2004) 51965
31. Stanley H.F., Kadwell M., and Wheeler J.C. Molecular evolution of the family Camelidae: a mitochondrial DNA study. Proc Biol Sci 256 (1994) 1
32. Tomlinson I.M., Walter G., Marks J.D., Llewelyn M.B., and Winter G. The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops. J Mol Biol 227 (1992) 776
33. van der Linden R., de Geus B., Stok W., Bos W., van Wassenaar D., Verrips T., and Frenken L. Induction of immune responses and molecular cloning of the heavy chain antibody repertoire of Lama glama. J Immunol Methods 240 (2000) 185
34. van der Linden R.H., Frenken L.G., de Geus B., Harmsen M.M., Ruuls R.C., Stok W., de Ron L., Wilson S., Davis P., and Verrips C.T. Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies. Biochim Biophys Acta 1431 (1999) 37
35. Verheesen P., Roussis A., de Haard H.J., Groot A.J., Stam J.C., den Dunnen J.T., Frants R.R., Verkleij A.J., Theo Verrips C., and van der Maarel S.M. Reliable and controllable antibody fragment selections from Camelid non-immune libraries for target validation. Biochim Biophys Acta 1764 (2006) 1307
36. Vu K.B., Ghahroudi M.A., Wyns L., and Muyldermans S. Comparison of llama VH sequences from conventional and heavy chain antibodies. Mol Immunol 34 (1997) 1121
37. Woolven B.P., Frenken L.G., van der Logt P., and Nicholls P.J. The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation. Immunogenetics 50 (1999) 98