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Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones

Cai, X; Wang, R; Filloux, A; Waksman, G; Meng, GY; (2011) Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones. PLOS ONE , 6 (1) , Article e16583. 10.1371/journal.pone.0016583. Green open access

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Abstract

Pseudomonas aeruginosa, an important human pathogen, is estimated to be responsible for,10% of nosocomial infections worldwide. The pathogenesis of P. aeruginosa starts from its colonization in the damaged tissue or medical devices (e. g. catheters, prothesis and implanted heart valve etc.) facilitated by several extracellular adhesive factors including fimbrial pili. Several clusters containing fimbrial genes have been previously identified on the P. aeruginosa chromosome and named cup [1]. The assembly of the CupB pili is thought to be coordinated by two chaperones, CupB2 and CupB4. However, due to the lack of structural and biochemical data, their chaperone activities remain speculative. In this study, we report the 2.5 A crystal structure of P. aeruginosa CupB2. Based on the structure, we further tested the binding specificity of CupB2 and CupB4 towards CupB1 (the presumed major pilus subunit) and CupB6 (the putative adhesin) using limited trypsin digestion and strep-tactin pull-down assay. The structural and biochemical data suggest that CupB2 and CupB4 might play different, but not redundant, roles in CupB secretion. CupB2 is likely to be the chaperone of CupB1, and CupB4 could be the chaperone of CupB4:CupB5:CupB6, in which the interaction of CupB4 and CupB6 might be mediated via CupB5.

Type: Article
Title: Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
Open access status: An open access version is available from UCL Discovery
DOI: 10.1371/journal.pone.0016583
Publisher version: http://dx.doi.org/10.1371/journal.pone.0016583
Language: English
Additional information: © 2011 Cai et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. This work was supported by "The Program for Professor of Special Appointment (Eastern Scholar) at Shanghai Institute of Higher Learning" (to GM), the research grants 31070645 and 30871105 of the National Natural Science Foundation of China (to GM and XC) and a research grant 08087 from the Wellcome Trust, the United Kingdom (to GM and GW). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Keywords: PILUS BIOGENESIS, PROTEIN SECRETION, USHER, BIOFILM, PATHWAYS, BACTERIA, COMPLEX, INFECTIONS, REFINEMENT, STRATEGIES
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1302120
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