Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1998-7-31
|
| pubmed:abstractText |
Self-tolerance, a key feature of the immune system, is still a matter of intense debate. We give here evidence for a peculiar behavior of an antiserum against Mycobacterium tuberculosis chaperonin 10 (m-Cpn10), which could have implications for the mechanism of self-recognition by antibodies against non-self. We show that this antiserum can interact in terms of both inhibition of biological activity and physical association (immunoprecipitation), with the mammalian homologue of m-Cpn10, but only if the bacterial protein is present. Several lines of evidence led us to exclude that the two proteins physically associate to form heterocomplexes: (1) the behavior of the antiserum was not shared by a monoclonal antibody against m-Cpn10; (2) a matrix selective for human Cpn10 (h-Cpn10) did not co-purify m-Cpn10; (3) the distribution pattern in non-denaturing isoelectric focusing of labeled m-Cpn10 was not altered by the presence of the unlabeled h-Cpn10. We conclude therefore that the antiserum against M. tuberculosis Cpn10 also recognizes mammalian Cpn10, with an affinity/avidity regulated by the mycobacterial protein, or by the promotion of hetero-oligomerization. This emergence of self-recognition in the presence of M. tuberculosis Cpn10 could imply a breaking of self-tolerance in situations of infection or vaccination.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
22
|
| pubmed:volume |
1403
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
151-7
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:9630589-Animals,
pubmed-meshheading:9630589-Antibodies, Bacterial,
pubmed-meshheading:9630589-Antibody Specificity,
pubmed-meshheading:9630589-Autoimmunity,
pubmed-meshheading:9630589-Chaperonin 10,
pubmed-meshheading:9630589-Cross Reactions,
pubmed-meshheading:9630589-Humans,
pubmed-meshheading:9630589-Mice,
pubmed-meshheading:9630589-Mycobacterium tuberculosis,
pubmed-meshheading:9630589-Protein Binding,
pubmed-meshheading:9630589-Self Tolerance,
pubmed-meshheading:9630589-Sequence Homology, Amino Acid,
pubmed-meshheading:9630589-Species Specificity
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Mycobacterial Cpn10 promotes recognition of the mammalian homologue by a mycobacterium-specific antiserum.
|
| pubmed:affiliation |
Istituto di Ricerche Farmacologiche 'Mario Negri', Via Eritrea 62, I-20157 Milan, Italy.
|
| pubmed:publicationType |
Journal Article
|