Molecular architecture of Streptococcus pneumoniae TIGR4 pili

Hilleringmann, M. and Ringler, P. and Müller, S. A. and De Angelis, G. and Rappuoli, R. and Ferlenghi, I. and Engel, A.. (2009) Molecular architecture of Streptococcus pneumoniae TIGR4 pili. The EMBO journal, Vol. 28, H. 24. pp. 3921-3930.

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Official URL: http://edoc.unibas.ch/dok/A5262452

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Although the pili of Gram-positive bacteria are putative virulence factors, little is known about their structure. Here we describe the molecular architecture of pilus-1 of Streptococcus pneumoniae, which is a major cause of morbidity and mortality worldwide. One major (RrgB) and two minor components (RrgA and RrgC) assemble into the pilus. Results from TEM and scanning transmission EM show that the native pili are approximately 6 nm wide, flexible filaments that can be over 1 microm long. They are formed by a single string of RrgB monomers and have a polarity defined by nose-like protrusions. These protrusions correlate to the shape of monomeric RrgB-His, which like RrgA-His and RrgC-His has an elongated, multi-domain structure. RrgA and RrgC are only present at the opposite ends of the pilus shaft, compatible with their putative roles as adhesin and anchor to the cell wall surface, respectively. Our structural analyses provide the first direct experimental evidence that the native S. pneumoniae pilus shaft is composed exclusively of covalently linked monomeric RrgB subunits oriented head-to-tail.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H and Müller, Shirley and Ringler, Philippe
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:01 Mar 2013 11:06
Deposited On:22 Mar 2012 13:24

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