Molecular Analysis of Putative Pneumococcal Virulence Proteins
- 1 January 1997
- journal article
- research article
- Published by Mary Ann Liebert Inc in Microbial Drug Resistance
- Vol. 3 (1), 1-10
- https://doi.org/10.1089/mdr.1997.3.1
Abstract
Although the polysaccharide capsule has been recognized as a sine qua non of virulence, recent attention has focused on the role of pneumococcal proteins in pathogenesis, particularly in view of their potential as vaccine antigens. The contribution of pneumolysin, two distinct neuraminidases, autolysin, hyaluronidase, and the 37 kDa pneumococcal surface adhesin A has been examined by specifically mutagenizing the respective genes in the pneumococcal chromosome and examining the impact on virulence in animal models. The vaccine potential of these proteins has also been assessed by immunization of mice with purified antigens, followed by challenge with virulent pneumococci.Keywords
This publication has 43 references indexed in Scilit:
- Protection of mice against fatal pneumococcal challenge by immunization with pneumococcal surface adhesin A (PsaA)Microbial Pathogenesis, 1996
- The contribution of pneumolysin to the pathogenicity of Streptococcus pneumoniaeTrends in Microbiology, 1996
- Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniaeMolecular Microbiology, 1996
- MOLECULAR ANALYSIS OF THE PATHOGENICITY OF STREPTOCOCCUS PNEUMONIAE: The Role of Pneumococcal ProteinsAnnual Review of Microbiology, 1993
- Comparative efficacy of autolysin and pneumolysin as immunogens protecting mice against infection by Streptococcus pneumoniaeMicrobial Pathogenesis, 1992
- Effect of insertional inactivation of the genes encoding pneumolysin and autolysin on the virulence of Streptococcus pneumoniae type 3Microbial Pathogenesis, 1992
- Structure and function of pneumolysin, the multifunctional, thiol‐activated toxin of Streptococcus pneumoniaeMolecular Microbiology, 1991
- Conserved sequences in bacterial and viral sialidasesGlycoconjugate Journal, 1989
- Use of insertional inactivation to facilitate studies of biological properties of pneumococcal surface protein A (PspA).The Journal of Experimental Medicine, 1987
- Neuraminidase activity in bacterial meningitisJournal of Clinical Investigation, 1971