Open AccessVersatility of choline metabolism and choline‐binding proteins in Streptococcus pneumoniae and commensal streptococci
Author(s) -
Hakenbeck Regine,
Madhour Abderrahim,
Denapaite Dalia,
Brückner Reinhold
Publication year - 2009
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.2009.00172.x
Subject(s) - streptococcus mitis , microbiology and biotechnology , streptococcus pneumoniae , phosphorylcholine , teichoic acid , biology , choline , lysin , lytic cycle , virulence , phosphocholine , cell wall , streptococcus , streptococcus oralis , bacterial cell structure , bacteria , peptidoglycan , biochemistry , bacteriophage , virology , virus , gene , phospholipid , escherichia coli , genetics , membrane , phosphatidylcholine , antibiotics
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.