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http://purl.uniprot.org/citations/19309566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19309566http://www.w3.org/2000/01/rdf-schema#comment"Internalin A (InlA), a cell wall-bound protein of Listeria monocytogenes, is among the major components involved in the adhesion to and invasion of host cells expressing specific forms of E-cadherin. Some L. monocytogenes strains secrete truncated non-functional forms of InlA. The purpose of this study is to compare the biofilm-forming abilities of L. monocytogenes strains from clinical sources expressing InlA proteins in the different forms. A total of 70 L. monocytogenes strains were examined using SDS-PAGE, Western blot, DNA sequencing, and microtitre plate biofilm formation assays. We found that 8 of the 70 strains expressed truncated InlA, and that this group of strains exhibited significantly enhanced biofilm-forming ability compared to the group expressing full-length InlA. Further experiments showed that: (i) L. monocytogenes biofilms were detached by treatment with protease K; (ii) protein fragments resulting from proteolysis, rather than intact proteins, are responsible for biofilm enhancement, because biofilm formation was impaired by the protease inhibitor alpha2-macroglobulin; (iii) truncated and/or proteolytically cleaved InlA are likely involved in the biofilm enhancement, based on the effects that anti-InlA monoclonal antibodies produced on the biofilm formation of L. monocytogenes strains expressing either truncated or full-length InlA. These data provide a basis for further investigation of the molecular structure and composition of L. monocytogenes biofilms."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.org/dc/terms/identifier"doi:10.1177/039463200902200121"xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/author"Aureli P."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/author"Franciosa G."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/author"Maugliani A."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/author"Scalfaro C."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/author"Floridi F."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/name"Int J Immunopathol Pharmacol"xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/pages"183-193"xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/title"Expression of internalin A and biofilm formation among Listeria monocytogenes clinical isolates."xsd:string
http://purl.uniprot.org/citations/19309566http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/19309566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19309566
http://purl.uniprot.org/citations/19309566http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19309566
http://purl.uniprot.org/uniprot/#_P0DJM0-mappedCitation-19309566http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19309566
http://purl.uniprot.org/uniprot/P0DJM0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19309566