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BslA, a pXO1‐encoded adhesin of Bacillus anthracis
Author(s) -
Kern Justin W.,
Schneewind Olaf
Publication year - 2008
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.1365-2958.2008.06169.x
Subject(s) - bacillus anthracis , biology , microbiology and biotechnology , virulence , plasmid , gene , pathogenicity island , genetics , bacteria
Summary The Gram‐positive pathogen Bacillus anthracis causes anthrax, a fulminant and lethal infection of mammals. Two large virulence plasmids, pXO1 and pXO2, harbour genes required for anthrax pathogenesis and encode secreted toxins or provide for the poly γ‐ d ‐glutamic acid capsule. In addition to capsule, B. anthracis harbours additional cell wall envelope structures, including the surface layer (S‐layer), which is composed of crystalline protein arrays. We sought to identify the B. anthracis envelope factor that mediates adherence of vegetative forms to human cells and isolated BslA ( B . anthracis S ‐ l ayer protein A ). Its structural gene, bslA , is located on the pXO1 pathogenicity island (pXO1‐90) and bslA expression is both necessary and sufficient for adherence of vegetative forms to host cells. BslA assembly into S‐layers and surface exposure is presumably mediated by three N‐terminal SLH domains. Twenty‐three B. anthracis genes, whose products harbour similar SLH domains, may provide additional surface molecules that allow bacilli to engage cells or tissues of specific hosts during anthrax pathogenesis.