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Structural basis of pilus anchoring by the ancillary pilin RrgC of Streptococcus pneumoniae.


ABSTRACT: Pili are surface-attached, fibrous virulence factors that play key roles in the pathogenesis process of a number of bacterial agents. Streptococcus pneumoniae is a causative agent of pneumonia and meningitis, and the appearance of drug-resistance organisms has made its treatment challenging, especially in developing countries. Pneumococcus-expressed pili are composed of three structural proteins: RrgB, which forms the polymerized backbone, RrgA, the tip-associated adhesin, and RrgC, which presumably associates the pilus with the bacterial cell wall. Despite the fact that the structures of both RrgA and RrgB were known previously, structural information for RrgC was still lacking, impeding the analysis of a complete model of pilus architecture. Here, we report the structure of RrgC to 1.85 Å and reveal that it is a three-domain molecule stabilized by two intradomain isopeptide bonds. RrgC does not depend on pilus-specific sortases to become attached to the cell wall; instead, it binds the preformed pilus to the peptidoglycan by employing the catalytic activity of SrtA. A comprehensive model of the type 1 pilus from S. pneumoniae is also presented.

SUBMITTER: Shaik MM 

PROVIDER: S-EPMC4059141 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Structural basis of pilus anchoring by the ancillary pilin RrgC of Streptococcus pneumoniae.

Shaik Md Munan MM   Maccagni Amandine A   Tourcier Guillaume G   Di Guilmi Anne Marie AM   Dessen Andréa A  

The Journal of biological chemistry 20140421 24


Pili are surface-attached, fibrous virulence factors that play key roles in the pathogenesis process of a number of bacterial agents. Streptococcus pneumoniae is a causative agent of pneumonia and meningitis, and the appearance of drug-resistance organisms has made its treatment challenging, especially in developing countries. Pneumococcus-expressed pili are composed of three structural proteins: RrgB, which forms the polymerized backbone, RrgA, the tip-associated adhesin, and RrgC, which presum  ...[more]

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