Linked Life Data

11163678

Source:http://linkedlifedata.com/resource/pubmed/id/11163678

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
2001-2-22
pubmed:abstractText
It is reported here that the PorB3 porin proteins of serotype 4 and 15 are poorly accessible for antibody binding on live Neisseria meningitidis bacteria, whereas the allelic PorB2 and the PorA outer membrane protein appear to be highly accessible. This was revealed by flow cytometry analysis using several mouse monoclonal antibodies (mAbs) as well as PorB3 specific antibodies isolated from post vaccination and patient sera. However, strong antibody binding to the PorB3 protein was observed after killing the bacteria with ethanol. The reason for the lack of epitope exposure could be a shielding effect of the carbohydrate chains of lipopolysaccharides (LPS) possibly combined with short extra-cellular loops in the PorB3 protein. The findings indicate that the PorB3 protein is not an optimal target for protective antibodies induced by vaccination.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0264-410X
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1526-33
pubmed:dateRevised
2011-4-7
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
PorB3 outer membrane protein on Neisseria meningitidis is poorly accessible for antibody binding on live bacteria.
pubmed:affiliation
Department of Vaccinology, National Institute of Public Health, P.O. Box 4404 Torshov, 0403, Oslo, Norway. terje.michaelsen@folkehelsa.no
pubmed:publicationType
Journal Article, In Vitro