Abstract
In the last two decades, discoveries in biological sciences have allowed vaccine research to expand rapidly. Progress in the understanding of the regulatory mechanisms of the immune response to infection, molecular biology, genomics, proteomics and bioinformatics have revolutionized the way vaccines are designed. Vaccinology has established its own credibility, and it is no longer only a subject in microbiology and immunology classes but a true complex discipline. Vaccines are no longer just crude and complex preparations of killed or attenuated microorganisms but can be defined as proteins, polysaccharides (Ps), or nucleic acids that are delivered to the immune system as single entities, as part of complex particles, or by live attenuated agents or vectors, thereby inducing specific responses that inactivate, destroy, or suppress pathogens1.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Plotkin SA, Orenstein WA. Preface. In: Plotkin SA, Orenstein WA, eds. Vaccines. 3rd ed. Philadelphia: W B Sanders Co., 1999.
Hoiseth S. Vaccines, Bacterial. In: Lederberg J, ed. Encyclopedia of Microbiology. 2nd ed. San Diego: Academic Press, 2000:767–778
Hayrinen J, Jennings H, Raff HV et al. Antibodies to polysialic acid and its N-propyl derivative: binding properties and interaction with human embryonal brain glycopeptides. J Infect Dis 1995; 171:1481–1490.
Finne J, Bitter-Suermann D, Goridis C et al. An IgG monoclonal antibody to group B meningococci cross-reacts with developmentally regulated polysialic acid units of glycoproteins in neural and extraneural tissues. J Immunol 1987; 138:4402–4407.
Martin D, Cadieux N, Hamel J et al. Highly conserved Neisseria meningitidis surface protein confers protection against experimental infection. J Exp Med 1997; 185:1173–1183.
Cadieux N, Plante M, Rioux CR et al. Bactericidal and cross-protective activities of a monoclonal antibody directed against Neisseria meningitidis NspA outer membrane protein. Infect Immun 1999; 67:4955–4959.
Martin D, Brodeur BR, Hamel J et al. Candidate Neisseria meningitidis NspA vaccine. J Biotechnol 2000; 83:27–31.
Plante M, Cadieux N, Rioux CR et al. Antigenic and molecular conservation of the gonococcal NspA protein. Infect Immun 1991; 67:2855–2861.
Moe GR, Tan S, Granoff DM. Differences in surface expression of NspA among Neisseria meningitidis group B strains. Infect Immun 1999; 67:5664–5675.
Moe GR, Zuno-Mitchell P, Lee SS et al. Functional activity of anti-Neisserial surface protein A monoclonal antibodies against strains of Neisseria meningitidis serogroup B. Infect Immun 2001; 69:3762–3771.
Maslanka SE, Gheesling LL, Libutti, DE. Standardization and a multilaboratory comparison of Neisseria meningitidis serogroup A and C serum bactericidal assays. Clin Diagn Lab Immunol 1997; 4:156–167.
Jansen C, Kuipers B, van der Biezen J et al. Immunogenicity of in vitro folded outer membrane protein PorA of Neisseria meningitidis. FEMS Immunol Med Microbiol 2000; 27:227–233.
Peeters CC, Claassen IJ, Schuller M et al. Immunogenicity of various presentation forms of PorA outer membrane protein of Neisseria meningitidis in mice. Vaccine 1999; 17:2702–2712.
Niebla O, Alvarez A, Martin A et al. Immunogenicity of recombinant class 1 protein from Neisseria meningitidis refolded into phospholipid vesicles and detergent. Vaccine 2001; 19:3568–3574.
Carnemate T, Mesa C, Menéndez T et al. Recombinant Opc protein from Neisseria meningitidis reconstitued into liposomes elicits opsonic antibodies following immunization. Biotechnol Appl Biochem 2001; 34:63–69.
Kasper DL, Paoletti LC, Wessels MR et al. Immune response to type III group B streptococcal polysaccharide-tetanus toxoid conjugate vaccine. J Clin Investig 1996; 98:2308–2314.
Lachenauer CS, Kasper DL, Shimada J et al. Serotypes VI and VIII predominate among group B streptococci isolated from pregnant Japanese women. J Infect Dis 1999; 179:1030–1033.
Brodeur BR, Boyer M, Charlebois I et al. Identification of group B streptococcal Sip protein, which elicits cross-protective immunity. Infect Immun 2000; 68:5610–5618.
Birkeland NK. Cloning, molecular characterization, and expression of the genes encoding the lytic functions of lactococcal bacteriophage phi LC3: a dual lysis system of modular design. Can J Microbiol 1994; 40:658–665.
Gravekamp C, Kasper DL, Paoletti LC et al. Alpha C protein as a carrier for type III capsular polysaccharide and as a protective protein in group B streptococcal vaccines. Infect Immun 1999; 67:2491–2496.
Stålhammar-Carlemalm M, Stenberg L, Lindahl G. Protein Rib: a novel group B streptococcal cell surface protein that confers protective immunity and is expressed by most strains causing invasive infections. J Exp Med 1993; 177:1593–1603.
Ferrieri P, Flores AE. Surface protein expression in group B streptococcal invasive isolates. Adv Exp Med Biol 1997; 418:635–637.
Larsson, C, Stålhammar-Carlemalm M, Lindahl G. Experimental vaccination against group B streptococcus, an encapsulated bacterium, with highly purified preparations of cell surface proteins Rib and α. Infect Immun 1996; 64:3518–3523.
Baker CJ, Kasper DL. Correlation fo maternal antibody deficiency with susceptibility to neonatal group B streptococcal infection. N Engl J Med 1976; 294:753–756
Baker CJ, Rench MA, Edwards MS et al. Immunization of pregnant women with a polysaccharide vaccine of group B Streptococcus. N Engl J Med 1988; 319:1180–1185.
Madoff LC, Paoletti LC, Tai JY et al. Maternal immunization of mice with group B streptococcal type III polysaccharide-beta C protein conjugate elicits protective antibody to multiple serotypes. J Clin Invest 1994; 94:286–292.
Martin D, Rioux S, Gagnon E et al. Protection from Group B streptococcal infection in neonatal mice by maternal immunization with recombinant Sip protein. Infect Immun 2002; 70:4897–4901
Hamel J, Charland N, Pineau I et al. Vaccination with newly identified pneumococcal conserved surface proteins confers protection against experimental pneumonia. Poster E-65. 2001. American Society for Microbiology 101st General Meeting, Orlando, FL.
Charland N, Martin D, Brodeur BR et al. Passive transfer of antibodies to pneumococcal BVH-3 and BVH-11 surface proteins prevented lethal experimental infection. Poster E-39. 2002. American Society for Microbiology 102nd General Meeting, Salt Lake City, UT.
Pautsch A, Schulz, GE. High-resolution structure of the OmpA membrane domain, J Mol Biol 2000; 298:273–282.
Guex N, Peitsch MC. SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modeling. Electrophoresis 1997; 18:2714–2723.
Rights and permissions
Copyright information
© 2003 Springer Science+Business Media New York
About this chapter
Cite this chapter
Brodeur, B.R., Martin, D., Rioux, S., Charland, N., Hamel, J. (2003). Universal Proteins As an Alternative Bacterial Vaccine Strategy. In: New Bacterial Vaccines. Medical Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0053-7_2
Download citation
DOI: https://doi.org/10.1007/978-1-4615-0053-7_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4902-0
Online ISBN: 978-1-4615-0053-7
eBook Packages: Springer Book Archive