2pz4

From Proteopedia

Revision as of 10:33, 23 January 2008

Crystal Structure of SpaB (GBS52), the minor pilin in gram-positive pathogen Streptococcus agalactiae

Overview

Streptococcus agalactiae is the leading cause of neonatal pneumonia, sepsis, and meningitis. The pathogen assembles heterotrimeric pilus, structures on its surface; however, their function in pathogenesis is, poorly understood. We report here the crystal structure of the pilin, GBS52, which reveals two IgG-like fold domains, N1 and N2. Each domain is, comprised of seven antiparallel beta strands, an arrangement similar to, the fold observed in the Staphylococcus aureus adhesin Cna. Consistent, with its role as an adhesin, deletion of gbs52 gene significantly reduces, bacterial adherence to pulmonary epithelial cells. Moreover, latex beads, linked to the GBS52 protein adhere to pulmonary but not to many other, epithelial cells; binding to the former is specifically inhibited by, antibodies against GBS52. Nonetheless, substantial binding is only, observed with N2 domain-conjugated beads. This study presents the, structure of a Gram-positive pilin that utilizes a distinct IgG fold, variant to mediate pathogen adherence to a specific tissue.

About this Structure

2PZ4 is a Single protein structure of sequence from Streptococcus agalactiae. Full crystallographic information is available from OCA.

Reference

An IgG-like domain in the minor pilin GBS52 of Streptococcus agalactiae mediates lung epithelial cell adhesion., Krishnan V, Gaspar AH, Ye N, Mandlik A, Ton-That H, Narayana SV, Structure. 2007 Aug;15(8):893-903. PMID:17697995

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