Universal antibodies and their applications to the quantitative determination of virtually all subtypes of the influenza A viral hemagglutinins

Vaccine

Volumn 26, Issue 48, 2008, Pages 6068-6076

  Chun, Stella ^a,d   Li, Changgui ^b   Van Domselaar, Gary ^c   Wang, Junzhi ^b   Farnsworth, Aaron ^a   Cui, Xiaoyu ^b   Rode, Harold ^a   Cyr, Terry D ^a   He, Runtao ^c   Li, Xuguang ^a,d  

^a Health Canada and World Health Organization Collaborating Center for Standardization and Evaluation of Biologicals   (Canada)

^b NATIONAL INSTITUTE FOR THE CONTROL OF PHARMACEUTICAL AND BIOLOGICAL PRODUCTS   (China)

^c PUBLIC HEALTH AGENCY OF CANADA   (Canada)

^d UNIVERSITY OF OTTAWA   (Canada)

Author keywords

Fusion peptide; Influenza vaccine; Potency testing; Protein unfolding; Universal antibodies

Indexed keywords

ANTIBODY; INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; PEPTIDE; VIRUS FUSION PROTEIN;

ANTIBODY PRODUCTION; ANTIBODY RESPONSE; ANTIGEN BINDING; ARTICLE; BIOINFORMATICS; CONJUGATION; ENZYME LINKED IMMUNOSORBENT ASSAY; HYDROPHOBICITY; IMMUNODIFFUSION; IMMUNOGENICITY; INFLUENZA VIRUS A; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; QUANTITATIVE ANALYSIS; VIRUS STRAIN; WESTERN BLOTTING;

ANTIBODIES; ANTIBODIES, VIRAL; ANTIBODY SPECIFICITY; BLOTTING, WESTERN; COMPUTATIONAL BIOLOGY; DATA INTERPRETATION, STATISTICAL; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; HEMAGGLUTININS, VIRAL; HUMANS; INFLUENZA A VIRUS; INFLUENZA B VIRUS; INFLUENZA VACCINES; PROTEIN CONFORMATION; PROTEIN DENATURATION; SOLUBILITY; VIRAL FUSION PROTEINS;

EID: 55049102432     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2008.09.015     Document Type: Article

References (39)

1. Poland G.A., Rottinghaus S.T., and Jacobson R.M. Influenza vaccines: a review and rationale for use in developed and underdeveloped countries. Vaccine 19 (2001) 2216-2220
2. Simonsen L., Taylor R.J., Viboud C., Miller M.A., and Jackson L.A. Mortality benefits of influenza vaccination in elderly people: an ongoing controversy. Lancet Infect Dis 7 (2007) 658-666
3. Carrat F., and Flahault A. Influenza vaccine: the challenge of antigenic drift. Vaccine 25 (2007) 6852-6862
4. Bridges C.B., Thompson W.W., Meltzer M.I., Reeve G.R., Talamonti W.J., Cox N.J., et al. Effectiveness and cost-benefit of influenza vaccination of healthy working adults: a randomized controlled trial. JAMA 284 (2000) 1655-1663
5. De Filette M., Min Jou W., Birkett A., Lyons K., Schultz B., Tonkyro A., et al. Universal influenza A vaccine: optimization of M2-based constructs. Virology 337 (2005) 149-161
6. Wood J.M., Dunleavy U., Newman R.W., Riley A.M., Robertson J.S., Minor P.D., et al. The influence of the host cell on standardisation of influenza vaccine potency. Dev Biol Stand 98 (1999) 183-188
7. World Health Organization. WHO Guidelines on the Use of Vaccines and Antivirals during Influenza Pandemics (2004), World Health Organization. Department of Communicable Disease Surveillance and Response, Geneva, Switzerland. WHO/CDS/CSR/RMD/2004.8 www.who.int
8. Zambon M.C. Epidemiology and pathogenesis of influenza. J Antimicrob Chemother Suppl. B (1999) 3-9
9. Skehel J.J., and Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69 (2000) 531-569
10. Friguet B., Chaffotte A.F., Djavadi-Ohaniance L., and Goldberg M.E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J Immunol Methods 77 (1985) 305-319
11. Horváth A., Tóth G.K., Gogolák P., Nagy Z., Kurucz I., Pecht I., et al. A hemagglutinin-based multipeptide construct elicits enhanced protective immune response in mice against influenza A virus infection. Immunol Lett 60 (1998) 127-136
12. Bianchi E., Liang X., Ingallinella P., Finotto M., Chastain M.A., Fan J., et al. Universal influenza B vaccine based on the maturational cleavage site of the hemagglutinin precursor. J Virol 79 (2005) 7380-7388
13. Gerhard W., Mozdzanowska K., and Zharikova D. Prospects for universal influenza virus vaccine. Emerg Infect Dis 12 (2006) 569-574
14. Nestorowicz A., Tregear G.W., Southwell C.N., Martyn J., Murray J.M., White D.O., et al. Antibodies elicited by influenza virus hemagglutinin fail to bind to synthetic peptides representing putative antigenic sites. Mol Immunol 22 (1985) 145-154
15. Schoofs P.G., Geysen H.M., Jackson D.C., Brown L.E., Tang X.L., and White D.O. Epitopes of an influenza viral peptide recognized by antibody at single amino acid resolution. J Immunol 140 (1988) 611-616
16. Jackson D.C., and Brown L.E. A synthetic peptide of influenza virus hemagglutinin as a model antigen and immunogen. Pept Res 4 (1991) 114-124
17. Scott D., Nitecki D.E., Kindler H., and Goodman J.W. Immunogenicity of biotinylated hapten-avidin complexes. Mol Immunol 21 (1984) 1055-1060
18. Stevens J., Blixt O., Tumpey T.M., Taubenberger J.K., Paulson J.C., and Wilson I.A. Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312 (2006) 404-410
19. Carr C.M., Chaudhry C., and Kim P.S. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc Natl Acad Sci USA 94 (1997) 14306-14313
20. Das Sarma J., Duttagupta C., Ali E., and Dhar T.K. Antibody to folic acid: increased specificity and sensitivity in ELISA by using epsilon-aminocaproic acid modified BSA as the carrier protein. J Immunol Methods 184 (1995) 1-6
21. Okawa Y., Howard C.R., and Steward M.W. Production of anti-peptide specific antibody in mice following immunization with peptides conjugated to mannan. J Immunol Methods 149 1 (1992) 127-131
22. Chen J., Lee K.H., Steinhauer D.A., Stevens D.J., Skehel J.J., and Wiley D.C. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95 (1998) 409-417
23. Atherton E., and Sheppard R.C. Solid-phase peptide synthesis, a practical approach (1989), IRL Press, Oxford, England
24. Röhm C., Zhou N., Süss J., Mackenzie J., and Webster R.G. Characterization of a novel influenza hemagglutinin, H15: criteria for determination of influenza A subtypes. Virology 217 (1996) 508-516
25. Fouchier R.A., Munster V., Wallensten A., Bestebroer T.M., Herfst S., Smith D., et al. Characterization of a novel influenza A virus hemagglutinin subtype (H16) obtained from black-headed gulls. J Virol 79 (2005) 2814-2822
26. World Health Organization. A revision of the system of nomenclature for influenza viruses: a WHO memorandum. Bull. WHO 58 (1980) 585-591
27. Wang K., Holtz K.M., Anderson K., Chubet R., Mahmoud W., and Cox M.M. Expression and purification of an influenza hemagglutinin-one step closer to a recombinant protein-based influenza vaccine. Vaccine 24 (2006) 2176-2185
28. Wu J., Amandoron E., Li X., Wainberg M.A., and Parniak M.A. Monoclonal antibody-mediated inhibition of HIV-1 reverse transcriptase polymerase activity. Interaction with a possible deoxynucleoside triphosphate binding domain. J Biol Chem 268 (1993) 9980-9985
29. Casley W.L., Ogrodowczyk C., Larocque L., Jaentschke B., LeBlanc-Westwood C., Menzies J.A., et al. Cytotoxic doses of ketoconazole affect expression of a subset of hepatic genes. J Toxicol Environ Health A 70 (2007) 1946-1955
30. Huang D., Pereboev A.V., Korokhov N., He R., Larocque L., Gravel C., et al. Significant alterations of biodistribution and immune responses in Balb/c mice administered with adenovirus targeted to CD40(+) cells. Gene Ther 15 (2008) 298-308
31. Findlay J.W., and Dillard R.F. Appropriate calibration curve fitting in ligand binding assays. AAPS J 9 (2007) E260-E267
32. Li K.B. ClustalW-MPI: ClustalW analysis using distributed and parallel computing. Bioinformatics 19 (2003) 1585-1586
33. Nagy Z., Rajnavölgyi E., Hollósi M., Tóth G.K., Váradi G., Penke B., et al. The intersubunit region of the influenza virus haemagglutinin is recognized by antibodies during infection. Scand J Immunol 40 (1994) 281-291
34. White J.M., and Wilson I.A. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J Cell Biol 105 6 Pt 2 (1987) 2887-2896
35. Daniels R.S., Downie J.C., Hay A.J., Knossow M., Skehel J.J., Wang M.L., et al. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40 (1985) 431-439
36. Aguado-Martínez A., Alvarez-García G., Arnaiz-Seco I., Innes E., and Ortega-Mora L.M. Use of avidity enzyme-linked immunosorbent assay and avidity Western blot to discriminate between acute and chronic Neospora caninum infection in cattle. J Vet Diagn Invest 17 (2005) 442-450
37. Klimashevskaya S., Obriadina A., Ulanova T., Bochkova G., Burkov A., Araujo A., et al. Distinguishing acute from chronic and resolved hepatitis C virus (HCV) infections by measurement of anti-HCV immunoglobulin G avidity index. J Clin Microbiol 45 (2007) 3400-3403
38. Swalley S.E., Baker B.M., Calder L.J., Harrison S.C., Skehel J.J., Wiley D.C., et al. Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation. Biochemistry 43 (2004) 5902-5911
39. Wood J.M., and Robertson J.S. From lethal virus to life-saving vaccine: developing inactivated vaccines for pandemic influenza. Nat Rev Microbiol 2 (2004) 842-847