Linked Life Data

8728353

Source:http://linkedlifedata.com/resource/pubmed/id/8728353

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-12-24
pubmed:abstractText
In this study, naturally-occurring, monoclonal IgM kappa anti-thymocyte autoantibodies from the neonatal inbred Balb/c mouse-derived hybridoma NMT-1 (NMT-1 mAb), previously reported to identify a restricted CD4+CD8+CD3/lo/int thymocyte subpopulation, have been shown to exhibit extensive polyspecificity. Using immunofluorescence, immunoblotting and antibody titration and competition ELISAs, NMT-1 mAbs exhibited polyspecific binding to 12 apparently structurally unrelated self and non-self antigens. The autoreactive component of the polyspecificity profile of NMT-1 mAbs encompassed reactivity to developmentally-related 14.5 and 18.3 kDa Thy-1 glycoforms expressed on a CD4+CD8+CD3-/lo/int thymocyte subpopulation. The autoreactivity profile of NMT-1 mAbs also included recognition of the heavy and light chains of mouse IgG1 and mouse cytokeratins within thymic medullary epithelium and basal epithelial cells of stratified squamous epithelium of mouse tongue, oesophagus, stomach, skin and vagina. Examination of the polyspecificity profile of NMT-1 mAbs was also undertaken using a panel of 23 antigens including heterologous proteins, phospholipids, haptens and bacterial antigens by antibody titration and competition ELISAs. Antibody titration ELISAs demonstrated that NMT-1 mAbs bound nine antigens including bovine carbonic anhydrase, ovalbumin, cardiolipin, phosphatidylserine, the haptens, DNP and FITC and the bacterial antigens including Escherichia coli beta-galactosidase and the toxoids from Corynebacterium tetani and Clostridium diphtheria. Competition ELISAs, based on the inhibition of NMT-1 mAb binding to antigens adsorbed to ELISA plate surfaces by inhibitor antigens in solution, demonstrated that NMT-1 mAb interactions were not dependent on multivalent binding. In these assays, NMT-1 mAbs recognized unmodified (native) epitopes on the solution phase forms of the protein antigens, including E. coli beta-galactosidase and toxoids from Corynebacterium tetani and Clostridium diphtheria, providing further evidence for the hypothesis that the binding of multiple, apparently unrelated, antigens by NMT-1 mAbs occurs via unique polyspecific antigen combining sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0165-6090
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-88
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8728353-Amino Acid Sequence, pubmed-meshheading:8728353-Animals, pubmed-meshheading:8728353-Antibodies, Monoclonal, pubmed-meshheading:8728353-Antibody Specificity, pubmed-meshheading:8728353-Antigens, CD3, pubmed-meshheading:8728353-Antigens, CD4, pubmed-meshheading:8728353-Antigens, CD8, pubmed-meshheading:8728353-Autoantibodies, pubmed-meshheading:8728353-B-Lymphocytes, pubmed-meshheading:8728353-Base Sequence, pubmed-meshheading:8728353-Cross Reactions, pubmed-meshheading:8728353-Hybridomas, pubmed-meshheading:8728353-Immunity, Innate, pubmed-meshheading:8728353-Mice, pubmed-meshheading:8728353-Mice, Inbred BALB C, pubmed-meshheading:8728353-Molecular Sequence Data, pubmed-meshheading:8728353-Rats, pubmed-meshheading:8728353-Rats, Wistar, pubmed-meshheading:8728353-Rheumatoid Factor, pubmed-meshheading:8728353-T-Lymphocyte Subsets, pubmed-meshheading:8728353-Thymus Gland
pubmed:year
1996
pubmed:articleTitle
Naturally-occurring anti-thymocyte autoantibody which identifies a restricted CD4+CD8+CD3-/lo/int thymocyte subpopulation exhibits extensive polyspecificity.
pubmed:affiliation
Department of Pathology, University of Melbourne, Parkville, Victoria, Australia. John_Underwood.pathology@muwaye. unimelb.edu.au
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't