Molecular architecture of Streptococcus pneumoniae TIGR4 pili

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 componen...

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Bibliographic Details
Published in:The EMBO journal 2009-12, Vol.28 (24), p.3921-3930
Main Authors: Hilleringmann, Markus, Ringler, Philippe, Müller, Shirley A, De Angelis, Gabriella, Rappuoli, Rino, Ferlenghi, Ilaria, Engel, Andreas
Format: Article
Language:English
Subjects:
Animals
Bacteria
Bacterial Adhesion
Bacterial Proteins - chemistry
Blotting, Western
Electrophoresis, Polyacrylamide Gel
EMBO23
EMBO40
Escherichia coli - metabolism
Fimbriae, Bacterial - metabolism
Gram-positive bacteria
mass measurement
Mice
Microbiology
Microscopy, Electron, Scanning - methods
Microscopy, Electron, Transmission - methods
Molecular biology
Morbidity
Mortality
Mutation
pilus
Polarity
Protein Conformation
Recombinant Proteins - chemistry
STEM
Streptococcus pneumoniae
Streptococcus pneumoniae - metabolism
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Summary: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 μm 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.
ISSN:0261-4189
1460-2075
DOI:10.1038/emboj.2009.360