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The SLH‐domain protein BslO is a determinant of Bacillus anthracis chain length
Author(s) -
Anderson Valerie J.,
Kern Justin W.,
McCool Justin W.,
Schneewind Olaf,
Missiakas Dominique
Publication year - 2011
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2011.07688.x
Subject(s) - biology , bacillus anthracis , mutant , bacilli , phenotype , homology (biology) , lysis , gene , virulence , microbiology and biotechnology , genetics , bacteria
Summary The Gram‐positive pathogen Bacillus anthracis grows in characteristic chains of individual, rod‐shaped cells. Here, we report the cell‐separating activity of BslO, a putative N ‐acetylglucosaminidase bearing three N‐terminal S‐layer homology (SLH) domains for association with the secondary cell wall polysaccharide (SCWP). Mutants with an insertional lesion in the bslO gene exhibit exaggerated chain lengths, although individual cell dimensions are unchanged. Purified BslO complements this phenotype in trans , effectively dispersing chains of bslO ‐deficient bacilli without lysis and localizing to the septa of vegetative cells. Compared with the extremely long chain lengths of csaB bacilli, which are incapable of binding proteins with SLH‐domains to SCWP , bslO mutants demonstrate a chaining phenotype that is intermediate between wild‐type and csaB . Computational simulation suggests that BslO effects a non‐random distribution of B. anthracis chain lengths, implying that all septa are not equal candidates for separation.