pubmed-article:16456881 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C0027575 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C0348801 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C0205470 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C1705241 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C0439097 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C1547348 | lld:lifeskim |
pubmed-article:16456881 | lifeskim:mentions | umls-concept:C0441836 | lld:lifeskim |
pubmed-article:16456881 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:16456881 | pubmed:dateCreated | 2006-3-13 | lld:pubmed |
pubmed-article:16456881 | pubmed:abstractText | We compared the proteome of detergent-derived group B Neisseria meningitidis (MenB) outer membrane vesicles (DOMVs) with the proteome of outer membrane vesicles (m-OMVs) spontaneously released into culture supernatant by MenB delta gna33, a mutant in which the gene coding for a lytic transglycosylase homologous to the E. coli MltA was deleted. In total, 138 proteins were identified in DOMVs by 1- and 2-DE coupled with MS; 64% of these proteins belonged to the inner membrane and cytoplasmic compartments. By contrast, most of the 60 proteins of m-OMVs were classified by PSORT as outer membrane proteins. When tested for their capacity to elicit bactericidal antibodies, m-OMVs elicited a broad protective activity against a large panel of MenB strains. Therefore, the identification of mutations capable of conferring an OMV-releasing phenotype in bacteria may represent an attractive approach to study bacterial membrane composition and organization, and to design new efficacious vaccine formulations. | lld:pubmed |
pubmed-article:16456881 | pubmed:language | eng | lld:pubmed |
pubmed-article:16456881 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16456881 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16456881 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16456881 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16456881 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16456881 | pubmed:month | Mar | lld:pubmed |
pubmed-article:16456881 | pubmed:issn | 1615-9853 | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:LDD | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:NoraisNathali... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:GaragusoIgnaz... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:GrandiGuidoG | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:Adu-BobieJean... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:GiulianiMarzi... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:PizzaMariagra... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:BiolchiAlessi... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:TaddeiAnna... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:FerrariGerman... | lld:pubmed |
pubmed-article:16456881 | pubmed:author | pubmed-author:DoroFrancesco... | lld:pubmed |
pubmed-article:16456881 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16456881 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:16456881 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16456881 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16456881 | pubmed:pagination | 1856-66 | lld:pubmed |
pubmed-article:16456881 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:16456881 | pubmed:meshHeading | pubmed-meshheading:16456881... | lld:pubmed |
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pubmed-article:16456881 | pubmed:meshHeading | pubmed-meshheading:16456881... | lld:pubmed |
pubmed-article:16456881 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16456881 | pubmed:articleTitle | Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles. | lld:pubmed |
pubmed-article:16456881 | pubmed:affiliation | Biochemistry and Molecular Biology Unit, Chiron Vaccines, Siena, Italy. | lld:pubmed |
pubmed-article:16456881 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16456881 | pubmed:publicationType | Comparative Study | lld:pubmed |
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