Self-assembling influenza nanoparticle vaccines elicit broadly neutralizing H1N1 antibodies

Nature

Volumn 499, Issue 7456, 2013, Pages 102-106

  Kanekiyo, Masaru ^a   Wei, Chih Jen ^a   Yassine, Hadi M ^a   McTamney, Patrick M ^a,b   Boyington, Jeffrey C ^a   Whittle, James R R ^a   Rao, Srinivas S ^a   Kong, Wing Pui ^a   Wang, Lingshu ^a   Nabel, Gary J ^a,c  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b MEDIMMUNE   (United States)

^c SANOFI   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FERRITIN; INACTIVATED VACCINE; INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; NEUTRALIZING ANTIBODY; POLYPEPTIDE; SELF ASSEMBLING INFLUENZA NANOPARTICLE VACCINE; UNCLASSIFIED DRUG;

ANTIBODY; CHEMICAL BINDING; IMMUNITY; INFLUENZA; NANOTECHNOLOGY; PROTEIN; PUBLIC HEALTH; VACCINE; VIRUS;

ANTIBODY TITER; ARTICLE; AUTOIMMUNITY; EXPRESSION VECTOR; FERRET; GENE FUSION; IMMUNE RESPONSE; IMMUNIZATION; IMMUNOGENICITY; IMMUNOLOGICAL TOLERANCE; INFLUENZA VIRUS A H1N1; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR BINDING; TRANSIENT TRANSFECTION; VIRUS SPIKE;

ANIMALS; ANTIBODIES, NEUTRALIZING; ANTIBODIES, VIRAL; BINDING SITES; CROSS REACTIONS; FEMALE; FERRETS; FERRITINS; HEMAGGLUTINATION INHIBITION TESTS; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; INFLUENZA A VIRUS, H1N1 SUBTYPE; INFLUENZA VACCINES; MALE; MICE; MICE, INBRED BALB C; NANOPARTICLES; ORTHOMYXOVIRIDAE INFECTIONS; VACCINES, INACTIVATED;

ANIMALIA; MUSTELA; ORTHOMYXOVIRIDAE;

EID: 84879882264     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12202     Document Type: Article

References (33)

1. Salomon, R. & Webster, R. G. The influenza virus enigma. Cell 136, 402-410 (2009).
2. Lambert, L. C. & Fauci, A. S. Influenza vaccines for the future. N. Engl. J. Med. 363, 2036-2044 (2010).
3. Yamashita, I. , Iwahori, K. &Kumagai, S. Ferritin in the field of nanodevices. Biochim. Biophys. Acta 1800, 846-857 (2010).
4. Ekiert, D. C. et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324, 246-251 (2009).
5. Sui, J. et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nature Struct. Mol. Biol. 16, 265-273 (2009).
6. Whittle, J. R. et al. Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc. Natl Acad. Sci. USA 108, 14216-14221 (2011).
7. Ekiert, D. C. et al. Cross-neutralization of influenza A viruses mediated by a single antibody loop. Nature 489, 526-532 (2012).
8. Wei, C. J. et al. Induction of broadly neutralizing H1N1 influenza antibodies by vaccination. Science 329, 1060-1064 (2010).
9. Ledgerwood, J. E. et al. DNA priming and influenza vaccine immunogenicity: two phase 1 open label randomised clinical trials. Lancet Infect. Dis. 11, 916-924 (2011).
10. Lee, L. A. & Wang, Q. Adaptations of nanoscale viruses and other protein cages for medical applications. Nanomedicine 2, 137-149 (2006).
11. Li, C. Q. , Soistman, E. &Carter, D. C. Ferritin nanoparticle technology. Anewplatform for antigen presentation and vaccine development. Ind. Biotechnol. 2, 143-147 (2006).
12. Meldrum, F. C. , Heywood, B. R. & Mann, S. Magnetoferritin: in vitro synthesis of a novel magnetic protein. Science 257, 522-523 (1992).
13. Jääskeläinen, A. et al. Production of apoferritin-based bioinorganic hybrid nanoparticles by bacterial fermentation followed by self-assembly. Small 3, 1362-1367 (2007).
14. Cho, K. J. et al. The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake. J. Mol. Biol. 390, 83-98 (2009).
15. O'Hagan, D. T. , Ott, G. S. , Nest, G. V. , Rappuoli, R. & Giudice, G. D. The history of MF59 adjuvant: a phoenix that arose from the ashes. Expert Rev. Vaccines 12, 13-30 (2013).
16. Mbow, M. L. , De Gregorio, E. , Valiante, N. M. & Rappuoli, R. New adjuvants for human vaccines. Curr. Opin. Immunol. 22, 411-416 (2010).
17. Nabel, G. J. & Fauci, A. S. Induction of unnatural immunity: prospects for a broadly protective universal influenza vaccine. Nature Med. 16, 1389-1391 (2010).
18. Okuno, Y. , Isegawa, Y. , Sasao, F. & Ueda, S. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67, 2552-2558 (1993).
19. Corti, D. et al. Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine. J. Clin. Invest. 120, 1663-1673 (2010).
20. Corti, D. et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856 (2011).
21. Ekiert, D. C. et al. A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333, 843-850 (2011).
22. Krause, J. C. et al. A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of influenza H1N1 virus hemagglutinin. J. Virol. 85, 10905-10908 (2011).
23. Lingwood, D. et al. Structural and genetic basis for development of broadly neutralizing influenza antibodies. Nature 489, 566-570 (2012).
24. Bachmann, M. F. & Zinkernagel, R. M. Neutralizing antiviral B cell responses. Annu. Rev. Immunol. 15, 235-270 (1997).
25. Xiong, A. S. et al. PCR-based accurate synthesis of long DNA sequences. Nature Protocols 1, 791-797 (2006).
26. Kong, W. P, et al. Protective immunity to lethal challenge of the 1918 pandemic influenza virus by vaccination. Proc. NatlAcad. Sci. USA103,15987-15991(2006).
27. Wei, C. J. et al. Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus. J. Virol. 82, 6200-6208 (2008).
28. Wei, C. J. et al. Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design. Sci. Transl. Med. 2, 24ra21 (2010).
29. Yang, Z. Y. et al. Immunization by avianH5influenza hemagglutininmutants with altered receptor binding specificity. Science 317, 825-828 (2007).
30. Wu, X. et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329, 856-861 (2010).
31. Zhou, T. et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329, 811-817 (2010).
32. Kong, W. P. et al. Immunogenicity of multiple gene and clade human immunodeficiency virus type 1DNA vaccines. J. Virol. 77, 12764-12772 (2003).
33. Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).