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A role for glycosylated serine-rich repeat proteins in Gram-positive bacterial pathogenesis

Authors


Carlos J. Orihuela, Associate Professor, Department of Microbiology and Immunology, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA Tel.: +1 210 567 3973; fax: +1 210 567 6612; E-mail: orihuela@uthscsa.edu

Summary

Bacterial attachment to host surfaces is a pivotal event in the biological and infectious processes of both commensal and pathogenic bacteria, respectively. Serine-rich repeat proteins (SRRPs) are a family of adhesins in Gram-positive bacteria that mediate attachment to a variety of host and bacterial surfaces. As such, they contribute towards a wide-range of diseases including sub-acute bacterial endocarditis, community-acquired pneumonia, and meningitis. SRRPs are unique in that they are glycosylated, require a non-canonical Sec-translocase for transport, and are largely composed of a domain containing hundreds of alternating serine residues. These serine-rich repeats are thought to extend a unique non-repeat (NR) domain outward away from the bacterial surface to mediate adhesion. So far, NR domains have been determined to bind to sialic acid moieties, keratins, or other NR domains of a similar SRRP. This review summarizes how this important family of bacterial adhesins mediates bacterial attachment to host and bacterial cells, contributes to disease pathogenesis, and might be targeted for pharmacological intervention or used as novel protective vaccine antigens. This review also highlights recent structural findings on the NR domains of these proteins.

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