pubmed-article:2509371 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0023810 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C1522138 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C0456570 | lld:lifeskim |
pubmed-article:2509371 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:2509371 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:2509371 | pubmed:dateCreated | 1989-12-21 | lld:pubmed |
pubmed-article:2509371 | pubmed:abstractText | A hybridoma line secreting a human monoclonal antibody (HMAb) capable of recognizing Fisher immunotype (IT) 1, 3, 4, and 6 lipopolysaccharide (LPS) in vitro was isolated. Peripheral blood lymphocytes (PBL) were obtained from volunteers immunized with an experimental Pseudomonas aeruginosa O polysaccharide-toxin A vaccine. PBL-expressing surface antibodies able to bind to P. aeruginosa LPS were isolated by adsorption onto LPS-coated plastic wells. Such PBL were transformed with Epstein-Barr virus. Lymphoblastoid cell lines secreting anti-P. aeruginosa LPS antibodies were identified by an enzyme-linked immunosorbent assay and fused to the F3B6 heteromyeloma line. A hybridoma line producing a HMAb (2-8AH79) able to bind IT-1, IT-3, IT-4, and IT-6 LPS was identified by an enzyme-linked immunosorbent assay. This HMAb was found to bind to the O-polysaccharide regions of IT-1, IT-3, IT-4, and IT-6 LPS, as determined by immunoblotting. By using an immunofluorescence microscopy assay, the cell surfaces of IT-3 and IT-4 bacteria were strongly stained by HMAb 2-8AH79, whereas those of IT-1 and IT-6 bacteria were weakly stained. This HMAb was found to promote the uptake and killing of IT-3 and IT-4 bacteria, but not IT-1 or IT-6 organisms, by human polymorphonuclear leukocytes. Similarly, the passive transfer of HMAb 2-8AH79 to mice afforded significant protection only against a challenge with IT-3 and IT-4 bacteria. | lld:pubmed |
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pubmed-article:2509371 | pubmed:language | eng | lld:pubmed |
pubmed-article:2509371 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2509371 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2509371 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2509371 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2509371 | pubmed:month | Dec | lld:pubmed |
pubmed-article:2509371 | pubmed:issn | 0019-9567 | lld:pubmed |
pubmed-article:2509371 | pubmed:author | pubmed-author:LarrickJ WJW | lld:pubmed |
pubmed-article:2509371 | pubmed:author | pubmed-author:FürerEE | lld:pubmed |
pubmed-article:2509371 | pubmed:author | pubmed-author:LangA BAB | lld:pubmed |
pubmed-article:2509371 | pubmed:author | pubmed-author:CryzS JSJJr | lld:pubmed |
pubmed-article:2509371 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2509371 | pubmed:volume | 57 | lld:pubmed |
pubmed-article:2509371 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2509371 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2509371 | pubmed:pagination | 3851-5 | lld:pubmed |
pubmed-article:2509371 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2509371 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2509371 | pubmed:articleTitle | Isolation and characterization of a human monoclonal antibody that recognizes epitopes shared by Pseudomonas aeruginosa immunotype 1, 3, 4, and 6 lipopolysaccharides. | lld:pubmed |
pubmed-article:2509371 | pubmed:affiliation | Swiss Serum and Vaccine Institute, Bern. | lld:pubmed |
pubmed-article:2509371 | pubmed:publicationType | Journal Article | lld:pubmed |
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