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http://purl.uniprot.org/citations/17041038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17041038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17041038http://www.w3.org/2000/01/rdf-schema#comment"Moraxella catarrhalis is a human-restricted pathogen that can cause respiratory tract infections. In this study, we identified a previously uncharacterized 24-kDa outer membrane protein with a high degree of similarity to Neisseria Opa protein adhesins, with a predicted beta-barrel structure consisting of eight antiparallel beta-sheets with four surface-exposed loops. In striking contrast to the antigenically variable Opa proteins, the M. catarrhalis Opa-like protein (OlpA) is highly conserved and constitutively expressed, with 25 of 27 strains corresponding to a single variant. Protease treatment of intact bacteria and isolation of outer membrane vesicles confirm that the protein is surface exposed yet does not bind host cellular receptors recognized by neisserial Opa proteins. Genome-based analyses indicate that OlpA and Opa derive from a conserved family of proteins shared by a broad array of gram-negative bacteria."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.org/dc/terms/identifier"doi:10.1128/JB.00788-06"xsd:string
http://purl.uniprot.org/citations/17041038http://purl.org/dc/terms/identifier"doi:10.1128/jb.00788-06"xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Hansen E.J."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Hansen E.J."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Gray-Owen S.D."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Gray-Owen S.D."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Brooks M.J."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Brooks M.J."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Laurence C.A."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/author"Laurence C.A."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/name"J Bacteriol"xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/pages"76-82"xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/pages"76-82"xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/title"Characterization of the Moraxella catarrhalis opa-like protein, OlpA, reveals a phylogenetically conserved family of outer membrane proteins."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/title"Characterization of the Moraxella catarrhalis opa-like protein, OlpA, reveals a phylogenetically conserved family of outer membrane proteins."xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/volume"189"xsd:string
http://purl.uniprot.org/citations/17041038http://purl.uniprot.org/core/volume"189"xsd:string
http://purl.uniprot.org/citations/17041038http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17041038
http://purl.uniprot.org/citations/17041038http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17041038