Identification of Major Outer Surface Proteins of Streptococcus agalactiae
AUTOR(ES)
Hughes, Martin J. G.
FONTE
American Society for Microbiology
RESUMO
To identify the major outer surface proteins of Streptococcus agalactiae (group B streptococcus), a proteomic analysis was undertaken. An extract of the outer surface proteins was separated by two-dimensional electrophoresis. The visualized spots were identified through a combination of peptide sequencing and reverse genetic methodologies. Of the 30 major spots identified as S. agalactiae specific, 27 have been identified. Six of these proteins, previously unidentified in S. agalactiae, were sequenced and cloned. These were ornithine carbamoyltransferase, phosphoglycerate kinase, nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase, purine nucleoside phosphorylase, enolase, and glucose-6-phosphate isomerase. Using a gram-positive expression system, we have overexpressed two of these proteins in an in vitro system. These recombinant, purified proteins were used to raise antisera. The identification of these proteins as residing on the outer surface was confirmed by the ability of the antisera to react against whole, live bacteria. Further, in a neonatal-animal model system, we demonstrate that some of these sera are protective against lethal doses of bacteria. These studies demonstrate the successful application of proteomics as a technique for identifying vaccine candidates.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=127763Documentos Relacionados
- Surface Proteins of Streptococcus agalactiae and Related Proteins in Other Bacterial Pathogens
- Surface protein of a Streptococcus agalactiae isolate.
- Regulation of expression of major outer surface proteins in Borrelia burgdorferi.
- Antigenic Determinants of Alpha-Like Proteins of Streptococcus agalactiae
- Identification of an immunologically important hypervariable domain of major outer surface protein A of Borrelia burgdorferi.