pubmed-article:18366441 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18366441 | lifeskim:mentions | umls-concept:C0004589 | lld:lifeskim |
pubmed-article:18366441 | lifeskim:mentions | umls-concept:C0243040 | lld:lifeskim |
pubmed-article:18366441 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:18366441 | pubmed:dateCreated | 2008-3-27 | lld:pubmed |
pubmed-article:18366441 | pubmed:abstractText | 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 gamma-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. anthracisS-layer 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. | lld:pubmed |
pubmed-article:18366441 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18366441 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18366441 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18366441 | pubmed:language | eng | lld:pubmed |
pubmed-article:18366441 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18366441 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18366441 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18366441 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18366441 | pubmed:month | Apr | lld:pubmed |
pubmed-article:18366441 | pubmed:issn | 1365-2958 | lld:pubmed |
pubmed-article:18366441 | pubmed:author | pubmed-author:SchneewindOla... | lld:pubmed |
pubmed-article:18366441 | pubmed:author | pubmed-author:KernJustin... | lld:pubmed |
pubmed-article:18366441 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18366441 | pubmed:volume | 68 | lld:pubmed |
pubmed-article:18366441 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18366441 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18366441 | pubmed:pagination | 504-15 | lld:pubmed |
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pubmed-article:18366441 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18366441 | pubmed:articleTitle | BslA, a pXO1-encoded adhesin of Bacillus anthracis. | lld:pubmed |
pubmed-article:18366441 | pubmed:affiliation | Department of Microbiology, University of Chicago, 920 East 58th Street, Chicago, IL, USA. | lld:pubmed |
pubmed-article:18366441 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18366441 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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