| The molecular switch that activates the cell wall anchoring step of pilus assembly in gram-positive bacteria. | |
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MedLine Citation:
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PMID: 18779588 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cell surface pili in gram-positive bacteria orchestrate the colonization of host tissues, evasion of immunity, and the development of biofilms. Recent work revealed that pilus assembly is a biphasic process wherein pilus polymerization is catalyzed by a pilus-specific sortase followed by cell wall anchoring of the pilus that is promoted by the housekeeping sortase. Here, we present molecular genetic and biochemical studies of a heterotrimeric pilus in Corynebacterium diphtheriae, uncovering the molecular switch that terminates pilus polymerization in favor of cell wall anchoring. The prototype pilus contains a major pilin (SpaA) forming the shaft, a tip pilin (SpaC), and another minor pilin (SpaB). Cells lacking SpaB form pilus fibers, but they are largely secreted in the medium, a phenotype also observed when cells lack the housekeeping sortase. Furthermore, the average pilus length is greatly increased in the absence of SpaB. Remarkably, a SpaB mutant that lacks the cell wall sorting signal but contains a critical lysine residue is incorporated in the pilus. However, the resulting pili fail to anchor to the cell wall. We propose that a specific minor pilin acts as the terminal subunit in pilus assembly. Cell wall anchoring ensues when the pilus polymer assembled on the pilus-specific sortase is transferred to the minor pilin presented by the housekeeping sortase via lysine-mediated transpeptidation. |
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Authors:
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Anjali Mandlik; Asis Das; Hung Ton-That |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2008-09-08 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 105 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2008 Sep |
Date Detail:
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Created Date: 2008-09-17 Completed Date: 2008-10-09 Revised Date: 2010-09-27 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 14147-52 Citation Subset: IM |
Affiliation:
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Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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genetics,
metabolism Biopolymers / metabolism Cell Wall / genetics, metabolism*, ultrastructure Corynebacterium diphtheriae / cytology*, genetics, metabolism* Cysteine Endopeptidases / genetics, metabolism Fimbriae, Bacterial / genetics, metabolism*, ultrastructure Membrane Proteins / genetics, metabolism Microscopy, Electron, Transmission Microscopy, Immunoelectron |
| Grant Support | |
ID/Acronym/Agency:
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AI061381/AI/NIAID NIH HHS; R01 AI061381-03/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Biopolymers; 0/Membrane Proteins; EC 3.4.22.-/Cysteine Endopeptidases |
| Comments/Corrections | |
Comment In:
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Proc Natl Acad Sci U S A. 2008 Sep 16;105(37):13703-4
[PMID:
18784365
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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