Structural vaccinology starts to deliver

Nature Reviews Microbiology

Volumn 10, Issue 12, 2012, Pages 807-813

  Dormitzer, Philip R ^a   Grandi, Guido ^b   Rappuoli, Rino ^b  

^a Novartis Vaccines and Diagnostics Inc   (United States)

^b NOVARTIS VACCINES AND DIAGNOSTICS   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; BINDING PROTEIN; COMPLEMENT FACTOR H; EPITOPE; FACTOR H BINDING PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; HYBRID PROTEIN; INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; MENINGOCOCCUS VACCINE; RESPIRATORY SYNCYTIAL VIRUS VACCINE; STREPTOCOCCUS VACCINE; UNCLASSIFIED DRUG; VACCINE; VIRUS GLYCOPROTEIN;

ANTIGENICITY; ARTICLE; DRUG DESIGN; HUMAN; IMMUNITY; IMMUNOGENICITY; NONHUMAN; PRIORITY JOURNAL; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS GROUP A; STRUCTURE ACTIVITY RELATION;

ANIMALS; ANTIGENS; DRUG DESIGN; EPITOPES; GENOMICS; HUMANS; VACCINES;

BACTERIA (MICROORGANISMS);

EID: 84869177341     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro2893     Document Type: Article

References (53)

1. Rappuoli, R., Mandl, C. W., Black, S. & De Gregorio, E. Vaccines for the twenty-first society. Nature Rev. Immunol. 11, 865-872 (2011).
2. Rappuoli, R. Reverse vaccinology. Curr. Opin. Microbiol. 3, 445-550 (2000).
3. Dormitzer, P. R., Ulmer, J. B. & Rappuoli, R. Structure-based antigen design: a strategy for next generation vaccines. Trends Biotechnol. 26, 659-667 (2008).
4. Masignani, V. et al. Vaccination against Neisseria meningitidis using three variants of the lipoprotein GNA1870. J. Exp. Med. 197, 789-799 (2003). (Pubitemid 36350873)
5. Scarselli, M. et al. Rational design of a meningococcal antigen inducing broad protective immunity. Sci. Transl. Med. 3, 91ra62 (2011).
6. Jiang, H. Q. et al. Broad vaccine coverage predicted for a bivalent recombinant factor H binding protein based vaccine to prevent serogroup B meningococcal disease. Vaccine 28, 6086-6093 (2010).
7. Fletcher, L. D. et al. Vaccine potential of the Neisseria meningitidis 2086 lipoprotein. Infect. Immun. 72, 2088-2100 (2004). (Pubitemid 38419922)
8. Giuliani, M. M. et al. A universal vaccine for serogroup B meningococcus. Proc. Natl Acad. Sci. USA 103, 10834-10839 (2006). (Pubitemid 44148381)
9. Mascioni, A. et al. Structural basis for the immunogenic properties of the meningococcal vaccine candidate LP2086. J. Biol. Chem. 284, 8738-8746 (2009).
10. Cantini, F. et al. Solution structure of the factor H-binding protein, a survival factor and protective antigen of Neisseria meningitidis. J. Biol. Chem. 284, 9022-9026 (2009).
11. Schneider, M. C. et al. Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates. Nature 458, 890-893 (2009).
12. Giuntini, S., Reason, D. C. & Granoff, D. M. Complement-mediated bactericidal activity of anti-factor H binding protein monoclonal antibodies against the meningococcus relies upon blocking factor H binding. Infect. Immun. 79, 3751-3759 (2011).
13. Scarselli, M. et al. Epitope mapping of a bactericidal monoclonal antibody against the factor H binding protein of Neisseria meningitidis. J. Mol. Biol. 386, 97-108 (2011).
14. Beernink, P. T. et al. A meningococcal factor H binding protein mutant that eliminates factor H binding enhances protective antibody responses to vaccination. J. Immunol. 186, 3606-3614 (2011).
15. Pajon, R., Beernink, P. T. & Granoff, D. M. Design of meningococcal factor H binding protein mutant vaccines that do not bind human complement factor H. Infect. Immun. 80, 2667-2677 (2012).
16. Beernink, P. T. & Granoff, D. M. Bactericidal antibody responses induced by meningococcal recombinant chimeric factor H-binding protein vaccines. Infect. Immun. 76, 2568-2575 (2008).
17. Edmond, K. M., et al. Group B streptococcal disease in infants aged younger than 3 months: systematic review and meta-analysis. Lancet 379, 547-556 (2012).
18. Lin, F. C. et al. Level of maternal IgG anti-group B Streptococcus type III antibody correlated with protection of neonates against early-onset disease caused by this pathogen. J. Infect. Dis. 190, 928-934 (2004).
19. Lauer, P. et al. Genome analysis reveals pili in Group B Streptococcus. Science 309, 105 (2005). (Pubitemid 40934983)
20. Mora, M. et al. Group A Streptococcus produce pilus-like structures containing protective antigens and Lancefield T antigens. Proc. Natl Acad. Sci. USA 102, 15641-15646 (2005). (Pubitemid 41528109)
21. Telford, J. L., Barocchi, M. A., Margarit, I., Rappuoli, R. & Grandi, G. Pili in Gram-positive pathogens. Nature Rev. Microbiol.4, 509-519 (2006). (Pubitemid 43905610)
22. Margarit, I. et al. Preventing bacterial infections with pilus-based vaccines: the group B Streptococcus paradigm. J. Infect. Dis. 199, 108-115 (2009).
23. Nuccitelli, A. et al. Structure-based approach to rationally design a chimeric protein for an effective vaccine against Group B Streptococcus infections. Proc. Natl Acad. Sci. USA 108, 10278-10283 (2011).
24. Stockman, L. J., Corns, A. T., Anderson, L. J. & Fischer-Langley, G. Respiratory syncytial virus-associated hospitalizations among infants and young children in the United States, 1997-2006. Pediatr. Infect. Dis. J. 31, 5-9 (2012).
25. Kim, H. W. et al. Respiratory syncytial virus disease in infants despite prior administration of antigenic inactivated vaccine. Am. J. Epidemiol. 89, 422-434 (1969).
26. Wright, P. F. et al. The absence of enhanced disease with wild type respiratory syncytial virus infection occurring after receipt of live, attenuated, respiratory syncytial virus vaccines. Vaccine 25, 7372-7378 (2007). (Pubitemid 47484016)
27. Swanson, K. A. et al. Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers. Proc. Natl Acad. Sci. USA 108, 9619-9624 (2011).
28. McLellan, J. S., Yang, Y., Graham, B. S. & Kwong, P. D. Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes. J. Virol. 85, 7788-7796 (2011).
29. Yin, H. S., Wen, X., Paterson, R. G., Lamb, R. A. & Jardetzky, T. S. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439, 38-44 (2006). (Pubitemid 43053622)
30. Magro, M. et al. Neutralizing antibodies against the preactive form of respiratory syncytial virus fusion protein offer unique possibilities for clinical intervention. Proc. Natl Acad. Sci. USA 109, 3089-3094 (2012).
31. Yin, H. S., Paterson, R. G., Wen, X., Lamb, R. A. & Jardetzky, T. S. Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein. Proc. Natl Acad. Sci. USA 102, 9288-9293 (2005). (Pubitemid 40923556)
32. Calder, L. J. et al. Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodies. Virology 271, 122-131 (2000). (Pubitemid 30341521)
33. Langley, J. M. et al. A dose-ranging study of a subunit Respiratory Syncytial Virus subtype A vaccine with and without aluminum phosphate adjuvantation in adults ≥65 years of age. Vaccine 27, 5913-5919 (2009).
34. Piedra, P. A. et al. Immunogenicity of a new purified fusion protein vaccine to respiratory syncytial virus: a multi-center trial in children with cystic fibrosis. Vaccine 21, 2448-2460 (2003). (Pubitemid 36561336)
35. McLellan, J. S. et al. Structural basis of respiratory syncytial virus neutralization by motavizumab. Nature Struct. Mol. Biol. 17, 248-250 (2010).
36. McLellan, J. S. et al. Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F. J. Virol. 84, 12236-12244 (2010).
37. López, J. A. et al. Conformational constraints of conserved neutralizing epitopes from a major antigenic area of human respiratory syncytial virus fusion glycoprotein. J. Gen. Virol. 74, 2567-2577 (1993). (Pubitemid 24020648)
38. Toiron, C. et al. Conformational studies of a short linear peptide corresponding to a major conserved neutralizing epitope of human respiratory syncytial virus fusion glycoprotein. Biopolymers 39, 537-548 (1996).
39. McLellan, J. S. et al. Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus. J. Mol. Biol. 409, 853-866 (2011).
40. Lingwood, D. et al. Structural and genetic basis for development of broadly neutralizing influenza antibodies. Nature 489, 566-571 (2012).
41. 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). (Pubitemid 23118850)
42. Ekiert, D. C. et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324, 246-251 (2009).
43. Throsby, M. et al. Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells. PLoS ONE 3, e3942 (2008).
44. 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).
45. 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).
46. Wiley, D. C., Wilson, I. A. & Skehel, J. J. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289, 373-378 (1981). (Pubitemid 11135143)
47. Whittle, J. R. 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).
48. Steel, J. et al. Influenza virus vaccine based on the conserved hemagglutinin stalk domain. MBio 1, e00018-e00010 (2010).
49. Liu, G. et al. Immunogenicity and efficacy of flagellin-fused vaccine candidates targeting 2009 pandemic H1N1 influenza in mice. PLoS ONE 6, e20928 (2011).
50. Song, L. et al. Efficacious recombinant influenza vaccines produced by high yield bacterial expression: a solution to global pandemic and seasonal needs. PLoS ONE 3, e2257 (2008).
51. Khurana, S. et al. Properly folded bacterially expressed H1N1 hemagglutinin globular head and ectodomain vaccines protect ferrets against H1N1 pandemic influenza virus. PLoS ONE 5, e11548 (2011).
52. McLellan, J. S. et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480, 336-343 (2011).
53. Johnson, S. et al. Design and evaluation of meningococcal vaccines through structure-based modification of host and pathogen molecules. 25 Oct 2012 (doi:10.1371/journal.ppat.1002981)