Source:http://linkedlifedata.com/resource/pubmed/id/11496013
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 8
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pubmed:dateCreated |
2001-8-9
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pubmed:databankReference | |
pubmed:abstractText |
Lipooligosaccharide (LOS) is a critical virulence factor of Neisseria meningitidis. A Tn916 insertion mutant, designated 469, was found to exhibit a markedly truncated LOS of 2.9 kDa when compared by Tricine/SDS-PAGE to the parental LOS (4.6 kDa). Electrospray mass spectrometry analysis of 469 LOS revealed that it consisted of the deep rough, heptose-deficient structure, Kdo(2)-lipid A. Sequencing of chromosomal DNA flanking the Tn916 insertion in mutant 469 revealed that the transposon had inserted into an ORF predicted to encode a 187 aa protein with sequence homology to the histidinol-phosphate phosphatase domain of Escherichia coli HisB and to a family of genes of unknown function. The gene, designated gmhX, is part of a polycistronic operon (ice-2) containing two other genes, nlaB and orfC. nlaB encodes a lysophosphatidic-acid acyltransferase and orfC is predicted to encode a N-acetyltransferase. Specific polar and non-polar gmhX mutations in the parental strain, NMB, exhibited the truncated LOS structure of mutant 469, and repair of gmhX mutants by homologous recombination with the wild-type gmhX restored the LOS parental phenotype. GmhX mutants demonstrated increased sensitivity to polymyxin B. GmhX mutants and other Kdo(2)-lipid A mutants also demonstrated increased sensitivity to killing by normal human serum but were not as sensitive as inner-core mutants containing heptose. In the genomes of Helicobacter pylori and Synechocystis, gmhX homologues are associated with heptose biosynthesis genes; however, in N. meningitidis, gmhX was found in a location distinct from that of gmhA, rfaD, rfaE, aut and rfaC. GmhX is a novel enzyme required for the incorporation of L-glycero-D-manno-heptose into meningococcal LOS, and is a candidate for the 2-D-glycero-manno-heptose phosphatase of the heptose biosynthesis pathway.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-deoxy-2-octulosonic...,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Transposable Elements,
http://linkedlifedata.com/resource/pubmed/chemical/Heptoses,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid A,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/glycero-manno-heptose,
http://linkedlifedata.com/resource/pubmed/chemical/lipid-linked oligosaccharides
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1350-0872
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
147
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2367-77
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11496013-Bacterial Proteins,
pubmed-meshheading:11496013-DNA Transposable Elements,
pubmed-meshheading:11496013-Genes, Bacterial,
pubmed-meshheading:11496013-Heptoses,
pubmed-meshheading:11496013-Lipid A,
pubmed-meshheading:11496013-Lipopolysaccharides,
pubmed-meshheading:11496013-Molecular Sequence Data,
pubmed-meshheading:11496013-Mutagenesis, Insertional,
pubmed-meshheading:11496013-Mutation,
pubmed-meshheading:11496013-Neisseria meningitidis,
pubmed-meshheading:11496013-Operon,
pubmed-meshheading:11496013-Phosphoric Monoester Hydrolases,
pubmed-meshheading:11496013-Sequence Analysis, DNA
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pubmed:year |
2001
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pubmed:articleTitle |
gmhX, a novel gene required for the incorporation of L-glycero-D-manno-heptose into lipooligosaccharide in Neisseria meningitidis.
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pubmed:affiliation |
Department of Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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