Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1995-6-22
pubmed:abstractText
Antibodies to partially purified E. coli 06 35-40 KDa porin trimers recognized the reactive epitopes in the intact porin surface molecule present in various wild-type, heterologous, urinary pathogens. The presence of lipopolysaccharide in the membrane did not shield the antibody binding sites. The reactivity was shown to be specific for porins since LPS-absorbed porin antisera reacted with porins on immunoblots and showed no reactivity with LPS. Additionally, the cross-reactions were abolished by absorption of the porin antisera with E. coli 06 containing porin trimers. These data strengthen the rationale for exploring the enhancement of immunoprotection by monoclonal antibodies to specific immunoreactive antigens in the porin molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0171-2985
pubmed:author
pubmed:issnType
Print
pubmed:volume
192
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
65-76
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Antibodies to Escherichia coli 06 porins cross-react with urinary pathogens.
pubmed:affiliation
Department of Urology, Tulane University School of Medicine, New Orleans, Louisiana, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.