pubmed-article:9600861 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9600861 | lifeskim:mentions | umls-concept:C0035588 | lld:lifeskim |
pubmed-article:9600861 | lifeskim:mentions | umls-concept:C1819995 | lld:lifeskim |
pubmed-article:9600861 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
pubmed-article:9600861 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:9600861 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
pubmed-article:9600861 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:9600861 | pubmed:dateCreated | 1998-7-9 | lld:pubmed |
pubmed-article:9600861 | pubmed:abstractText | rOmpA and rOmpB are immunodominant, surface-exposed proteins of Rickettsia rickettsii. Prior evidence suggests that adhesion of R. rickettsii to the host cell is mediated by a rickettsial protein. Five monoclonal antibodies to rOmpA, five to rOmpB, and one to the rickettsial lipopolysaccharide (LPS) were tested for inhibition of rickettsial attachment. All the monoclonal antibodies to rOmpA inhibited adhesion of rickettsiae to the L-929 cells with some inhibition rates as high as 90%. In contrast, monoclonal antibodies to rOmpB and LPS did not block attachment. When Fab fragments of monoclonal antibodies against rOmpA and rOmpB were used, similar results were observed as for the intact monoclonals, non-adhesion and adhesion, respectively. Purified rOmpA showed a competitive inhibitive effect on the attachment of R. rickettsii to host cells. Trypsin completely digested rOmpA but not rOmpB from the surface of intact R. rickettsii, resulting in loss of the ability of the rickettsiae to attach to the host cell. rOmpA appears to play an important role in the initial adhesion of R. rickettsii to the host cell. | lld:pubmed |
pubmed-article:9600861 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:language | eng | lld:pubmed |
pubmed-article:9600861 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9600861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9600861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600861 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9600861 | pubmed:month | May | lld:pubmed |
pubmed-article:9600861 | pubmed:issn | 0882-4010 | lld:pubmed |
pubmed-article:9600861 | pubmed:author | pubmed-author:WalkerD HDH | lld:pubmed |
pubmed-article:9600861 | pubmed:author | pubmed-author:LiHH | lld:pubmed |
pubmed-article:9600861 | pubmed:copyrightInfo | Copyright 1998 Academic Press Limited. | lld:pubmed |
pubmed-article:9600861 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9600861 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:9600861 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9600861 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9600861 | pubmed:pagination | 289-98 | lld:pubmed |
pubmed-article:9600861 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:9600861 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9600861 | pubmed:articleTitle | rOmpA is a critical protein for the adhesion of Rickettsia rickettsii to host cells. | lld:pubmed |
pubmed-article:9600861 | pubmed:affiliation | Department of Pathology, The University of Texas Medical Branch, Galveston, TX, 77555-0609, USA. | lld:pubmed |
pubmed-article:9600861 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9600861 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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