Human TNF cytokine neutralization with a vNAR from Heterodontus francisci shark

mAbs

Volumn 5, Issue 1, 2013, Pages 80-85

  Camacho Villegas, Tanya ^a,b   Mata Gonzalez, Teresa ^c   Paniagua Solis, Jorge ^c,d   Sanchez, Edna ^b   Licea, Alexei ^b  

^a UNIVERSIDAD AUTÓNOMA DE BAJA CALIFORNIA   (Mexico)

^b CENTRO DE INVESTIGACIÓN CIENTÍFICA Y DE EDUCACIÓN SUPERIOR DE ENSENADA   (Mexico)

^c Laboratorios Silanes SA de CV   (Mexico)

^d Parque Científico de Madrid   (Spain)

Author keywords

Heterodontus francisci; IgNAR; Neutralization; RhTNF ; Shark; Single domain antibodies; VNAR

Indexed keywords

NEUTRALIZING ANTIBODY; RECOMBINANT TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VNAR ANTIBODY;

ANIMAL EXPERIMENT; ANTIBODY ISOLATION; ARTICLE; CLONE; CONTROLLED STUDY; CYTOPLASM; HETERODONTUS FRANCISCI; IMMUNIZATION; IN VITRO STUDY; MALE; NONHUMAN; PHAGE DISPLAY; PROTEIN DOMAIN; PROTEIN EXPRESSION; SHARK;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, NEUTRALIZING; ANTIBODY SPECIFICITY; HUMANS; IMMUNIZATION; IMMUNOGLOBULIN VARIABLE REGION; IMMUNOGLOBULINS; MALE; MICE; MOLECULAR SEQUENCE DATA; NEUTRALIZATION TESTS; PEPTIDE LIBRARY; RECOMBINANT PROTEINS; SHARKS; SHOCK, SEPTIC; SINGLE-DOMAIN ANTIBODIES; TUMOR NECROSIS FACTOR-ALPHA;

EID: 84872852390     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.22593     Document Type: Article

References (21)

1. Deffar K, Shi H, Li L., Wang X, Zhu X. Nanobodies: the new concept in antibody engineering. Afr J Biotechnol 2009; 8:2645-52
2. Wesolowski J, Alzogaray V, Reyelt J., Unger M, Juarez K, Urrutia M., et al Single domain antibodies: promising experimental and therapeutic tools in infection and immunity. Med Microbiol Immunol 2009; 198:157-74; PMID:19529959; http://dx.doi.org/10.1007/s00430-009-0116-7
3. Hudson PJ, Souriau C. Engineered antibodies. Nat Med 2003; 9:129-34; PMID:12514726; http://dx.doi.org/10.1038/nm0103-129
4. Dooley H, Flajnik M F, Porter AJ Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display. Mol Immunol 2003; 40:25-33; PMID:12909128; http://dx.doi.org/10.1016/S0161-5890(03)00084-1
5. Roux KH, Greenberg AS, Greene L, Strelets L., Avila D, McKinney EC, et al Structural analysis of the nurse shark (new) antigen receptor (NAR): molecular convergence of NAR and unusual mammalian immunoglobulins. Proc Natl Acad Sci USA 1998; 95:11804-9; PMID:9751746; http://dx.doi.org/10.1073/pnas.95.20.11804
6. Greenberg AS, Avila D, Hughes M., Hughes A, McKinney EC, Flajnik M F. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature 1995; 374:168-73; PMID:7877689; http://dx.doi.org/10.1038/374168a0
7. Nuttall SD, Krishnan U V, Hattarki M, De Gori R, Irving RA, Hudson PJ Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries. Mol Immunol 2001; 38:313-26; PMID:11566324; http://dx.doi.org/10.1016/S0161-5890(01)00057-8
8. Stanfield RL, Dooley H, Flajnik M F, Wilson IA Crystal structure of a shark single-domain antibody V region in complex with lysozyme. Science 2004; 305:1770-3; PMID:15319492; http://dx.doi.org/10.1126/science.1101148
9. Simmons D.P., Streltsov VA, Dolezal O, Hudson P.J., Coley AM, Foley M, et al Shark IgNAR antibody mimotopes target a murine immunoglobulin through extended CDR3 loop structures. Proteins 2008; 71:119-30; PMID:17932913; http://dx.doi.org/10.1002/prot.21663
10. Nuttall SD, Krishnan UV, Doughty L, Nathanielsz A., Ally N, Pike RN, et al A naturally occurring NAR variable domain binds the Kgp protease from Porphyromonas gingivalis. FEBS Lett 2002; 516:80-6; PMID:11959108; http://dx.doi.org/10.1016/S0014-5793(02)02506-1
11. Juarez K, Dubberke G, Lugo P., Koch-Nolte F, Buck F, Haag F., et al Monoclonal antibodies for the identification and purification of vNAR domains and IgNAR immunoglobulins from the horn shark Heterodontus francisci. Hybridoma (Larchmt) 2011; 30:323-9; PMID:21851231; http://dx.doi.org/10.1089/hyb.2011.0010
12. Van Bockstaele F., Holz JB, Revets H. The development of nanobodies for therapeutic applications. Curr Opin Investig Drugs 2009; 10:1212-24; PMID:19876789
13. Gay RD, Clarke AW, Elgundi Z, Domagala T., Simpson RJ, Le NB, et al Anti-TNFα domain antibody construct CEP-37247: Full antibody functionality at half the size. MAbs 2010; 2:625-38; PMID:20930515; http://dx.doi.org/10. 4161/mabs.2.6.13493
14. Coppieters K, Dreier T, Silence K., de Haard H, Lauwereys M, Casteels P., et al Formatted anti-tumor necrosis factor alpha VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen-induced arthritis. Arthritis Rheum 2006; 54:1856-66; PMID:16736523; http://dx.doi.org/10.1002/art.21827
15. Ducourau E, Mulleman D, Paintaud G., Miow Lin DC, Lauféron F, Ternant D., et al Antibodies toward infliximab are associated with low infliximab concentration at treatment initiation and poor infliximab maintenance in rheumatic diseases. Arthritis Res Ther 2011; 13:R105; PMID:21708018; http://dx.doi.org/10.1186/ar3386
16. Thalayasingam N, Isaacs JD Anti-TNF therapy. Best Pract Res Clin Rheumatol 2011; 25:549-67; PMID:22137924; http://dx.doi.org/10.1016/j.berh.2011. 10.004
17. Kim SJ, Park Y, Hong HJ Antibody engineering for the development of therapeutic antibodies. Mol Cells 2005; 20:17-29; PMID:16258237
18. Fennell BJ, Darmanin-Sheehan A, Hufton S.E., Calabro V., Wu L, Müller MR, et al Dissection of the IgNAR V domain: molecular scanning and orthologue database mining define novel IgNAR hallmarks and affinity maturation mechanisms. J Mol Biol 2010; 400:155-70; PMID:20450918; http://dx.doi.org/10. 1016/j.jmb.2010.04.061
19. Sivashanmugam A, Murray V, Cui C., Zhang Y, Wang J, Li Q. Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci 2009; 18:936-48; PMID:19384993; http://dx.doi.org/10.1002/pro.102
20. Barbas C.F., Burton DR, Scott JK Phage Display: A Laboratory Manual. New York. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. 2001
21. Minsky A, Summers RG, Knowles JR Secretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a distinct release step associated with a conformational change. Proc Natl Acad Sci USA 1986; 83:4180-4; PMID:3520569; http://dx.doi.org/10.1073/pnas.83.12.4180