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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-11-9
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pubmed:databankReference | |
pubmed:abstractText |
Bacillus anthracis produces a gamma-linked poly-D-glutamic acid capsule that is essential for virulence. A 6.2 kb fragment of B. anthracis DNA (cap), when present in Escherichia coli, produces a capsular polymer that is immunologically identical to that produced by B. anthracis. By immunodiffusion analysis of E. coli strains carrying varying portions of the cap region, we identified a novel gene (dep) responsible for degradation of the capsular polymer of B. anthracis. The simultaneous presence of the cap region and the dep gene caused production of low-molecular-weight, degraded capsular polymer both in E. coli and in B. anthracis, whereas the cap region alone caused production of a high-molecular-weight capsule. The dep gene mapped immediately downstream of the cap region within a 1.8 kb fragment and was transcribed in the same direction. This fragment was sequenced and a 1401 bp open reading frame (ORF) was found that is predicted to encode a peptide with molecular weight of 51,460. By in vitro transcription-translation analysis, this ORF was shown to be the dep gene product. The deduced amino acid sequence of the dep product has sequence similarity to E. coli and mammalian gamma-glutamyltranspeptidase (GGT). However, the Dep protein did not have GGT activity. The Dep protein appears to be an enzyme that catalyses the hydrolysis of the poly-D-glutamic acid capsule. Although the biological functions of the dep gene are unknown, it is possible that low-molecular-weight, diffusible polyglutamates produced through the action of the dep gene may act to inhibit host defence mechanisms.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Capsules,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-Glutamyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:geneSymbol |
dep
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
487-96
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8105361-Amino Acid Sequence,
pubmed-meshheading:8105361-Bacillus anthracis,
pubmed-meshheading:8105361-Bacterial Capsules,
pubmed-meshheading:8105361-Bacterial Proteins,
pubmed-meshheading:8105361-Base Sequence,
pubmed-meshheading:8105361-Escherichia coli,
pubmed-meshheading:8105361-Genes, Bacterial,
pubmed-meshheading:8105361-Molecular Sequence Data,
pubmed-meshheading:8105361-Mutagenesis, Insertional,
pubmed-meshheading:8105361-Peptides,
pubmed-meshheading:8105361-Recombinant Proteins,
pubmed-meshheading:8105361-Sequence Analysis, DNA,
pubmed-meshheading:8105361-Sequence Homology, Amino Acid,
pubmed-meshheading:8105361-gamma-Glutamyltransferase
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pubmed:year |
1993
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pubmed:articleTitle |
Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis.
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pubmed:affiliation |
National Institute of Animal Health, Tsukuba Science City, Ibaraki, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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