Document Detail

Cell surface display of minor pilin adhesins in the form of a simple heterodimeric assembly in Corynebacterium diphtheriae.
MedLine Citation:
PMID:  21205008     Owner:  NLM     Status:  MEDLINE    
Pilus assembly in Gram-positive bacteria occurs by a two-step mechanism, whereby pilins are polymerized and then covalently anchored to the cell wall. In Corynebacterium diphtheriae, the pilin-specific sortase SrtA catalyses polymerization of the SpaA-type pilus, consisting of the shaft pilin SpaA, tip pilin SpaC and minor pilin SpaB. Cell wall anchoring of the SpaA polymers is triggered when SrtA incorporates SpaB into the pilus base via lysine-mediated transpeptidation; anchoring to the cell wall peptidoglycan is subsequently catalysed by the housekeeping sortase SrtF. Here we show that SpaB and SpaC formed a heterodimer independent of SpaA polymerization. SrtA was absolutely required for the formation of the SpaBC heterodimer, while SrtF facilitated the optimal cell wall anchoring of this heterodimer. Alanine substitution of the SpaB lysine residue K139 or truncation of the SpaB cell wall-sorting signal (CWSS) abolished assembly of the SpaBC heterodimer, hence underscoring SpaB function in transpeptidation and cell wall linkage. Importantly, sortase specificity for the cell wall-anchoring step was found to be dependent on the LAFTG motif within the SpaB CWSS. Thus, C. diphtheriae employs a common sortase-catalysed mechanism involving lysine-mediated transpeptidation to generate both adhesive pilus and simple heterodimeric structures on the bacterial the cell wall.
Chungyu Chang; Anjali Mandlik; Asis Das; Hung Ton-That
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-01-05
Journal Detail:
Title:  Molecular microbiology     Volume:  79     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-02-22     Completed Date:  2011-06-01     Revised Date:  2014-09-10    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1236-47     Citation Subset:  IM    
Copyright Information:
© 2011 Blackwell Publishing Ltd.
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MeSH Terms
Adhesins, Bacterial / chemistry,  genetics,  metabolism*
Aminoacyltransferases / genetics,  metabolism
Bacterial Proteins / genetics,  metabolism
Cell Wall / chemistry,  genetics,  metabolism*
Corynebacterium diphtheriae / chemistry,  enzymology,  genetics,  metabolism*
Cysteine Endopeptidases / genetics,  metabolism
Fimbriae Proteins / chemistry,  genetics,  metabolism*
Grant Support
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Bacterial Proteins; 147680-16-8/Fimbriae Proteins; EC 2.3.2.-/Aminoacyltransferases; EC 2.3.2.-/sortase A; EC 3.4.22.-/Cysteine Endopeptidases

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