Versatility of pneumococcal surface proteins.
Surface-exposed proteins are key players during the infectious process of pathogenic bacteria. The cell surface of the Gram-positive human pathogen Streptococcus pneumoniae is decorated not only by typical Gram-positive surface proteins, but also by a family of proteins that recognizes the phosphorylcholine of the lipoteichoic and teichoic acids, namely the choline-binding proteins, and by non-classical surface proteins that lack a leader peptide and membrane-anchor motif. A comprehensive understanding of how microbial proteins subvert host immunity or host protein functions is a prerequisite for the development of novel therapeutic strategies to combat pneumococcal infections. This article reviews recent progress in the investigation of the versatility and sophistication of the virulence functions of surface-exposed pneumococcal proteins.
Bergmann
Simone
S
Research Center for Infectious Diseases, University of Würzburg, Röntgenring 11, D-97070 Würzburg, Germany.
Hammerschmidt
Sven
S
Research Center for Infectious Diseases, University of Würzburg, Röntgenring 11, D-97070 Würzburg, Germany.
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D001665:Binding Sites; D002473:Cell Wall / Q000378:metabolism; D016680:Genome, Bacterial; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013296:Streptococcus pneumoniae / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D014774:Virulence
D001425:Bacterial Outer Membrane Proteins; D010457:Peptidoglycan