Versatility of choline metabolism and choline-binding proteins in Streptococcus pneumoniae and commensal streptococci

被引:65
作者
Hakenbeck, Regine [1 ]
Madhour, Abderrahim [1 ]
Denapaite, Dalia [1 ]
Brueckner, Reinhold [1 ]
机构
[1] Univ Kaiserslautern, Dept Microbiol, D-67663 Kaiserslautern, Germany
关键词
Streptococcus pneumoniae; Streptococcus oralis; Streptococcus mitis; choline-binding proteins; teichoic acid; ACID PHOSPHORYLCHOLINE ESTERASE; PNEUMOCOCCAL LIPOTEICHOIC ACID; ANTIGEN C-POLYSACCHARIDE; LYTIC ENZYME CPL-1; GROUP-O-ANTIGEN; TEICHOIC-ACID; CELL-WALL; SURFACE PROTEIN; ALLELIC VARIATION; MOLECULAR CHARACTERIZATION;
D O I
10.1111/j.1574-6976.2009.00172.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The pneumococcal choline-containing teichoic acids are targeted by choline-binding proteins (CBPs), major surface components implicated in the interaction with host cells and bacterial cell physiology. CBPs also occur in closely related commensal species, Streptococcus oralis and Streptococcus mitis, and many strains of these species contain choline in their cell wall. Physiologically relevant CBPs including cell wall lytic enzymes are highly conserved between Streptococcus pneumoniae and S. mitis. In contrast, the virulence-associated CBPs, CbpA, PspA and PcpA, are S. pneumoniae specific and are thus relevant for the characteristic properties of this species.
引用
收藏
页码:572 / 586
页数:15
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