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FEMS Microbiol Rev. 2009 May;33(3):572-86.

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

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1
Department of Microbiology, University of Kaiserslautern, Germany. hakenb@rhrk.uni-kl.de

Abstract

The pneumococcal choline-containing teichoic acids are targeted by cholinebinding 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.

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