Linked Life Data

1378932

Source:http://linkedlifedata.com/resource/pubmed/id/1378932

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7-8
pubmed:dateCreated
1992-8-26
pubmed:abstractText
The immune recognition of a molecule naturally presented as a monomeric or an oligomeric structure is analyzed using the human chorionic gonadotropin alpha subunit (hCG-alpha) as a model. Indeed, hCG-alpha circulates as either a free subunit or combined to the beta subunit (hCG-beta) to form the dimeric hCG hormone. A T cell study was performed in BALB/c (H-2d) mice which were found to be high responders to hCG-alpha. Mice were immunized with the free hCG-alpha or the dimeric hCG alpha/beta, and their lymph node cells were challenged in vitro with either alpha subunits from different species, hCG or peptides spanning the entire primary structure of hCG-alpha. Proliferation and IL-2 assays demonstrated that hCG-alpha-primed lymph node cells responded equally well to hCG-alpha and hCG alpha/beta, suggesting that both the free and combined hCG-alpha subunits are processed in a similar way. Among the various synthetic peptides used, only those mimicking the hCG-alpha(59-92) C-terminus portion were able to stimulate hCG-alpha-primed lymph node cells, demonstrating that this region contains immunodominant T cell recognition site(s). The hCG-alpha(23-43) and (32-59) peptides, although incapable of stimulating T cells primed with hCG-alpha, elicited a T cell response when used as immunogens. These regions encompassed cryptic epitopes which were not generated during hCG-alpha processing in H-2d mice. The T cell epitopes of hCG-alpha above described as immunodominant or cryptic on the free alpha subunit, had similar characteristics when the alpha/beta dimer was used as the immunogen. In contrast, T cells primed with peptides mimicking immunodominant sites recognized differently the hCG-alpha and the hCG alpha/beta antigens. Moreover, the analysis of the B cell response to all the immunogenic hCG-alpha peptides indicated that they bear B and T cell epitopes as well. Antibodies elicited against the hCG-alpha(59-92) or (32-59) peptide were capable of recognizing the alpha subunit in its free form but not in the alpha/beta hCG dimer. Such study deserves attention for the comprehensive mechanisms of the immune response to hCG as well as for the design of anti-hCG vaccines.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
883-93
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1378932-Amino Acid Sequence, pubmed-meshheading:1378932-Animals, pubmed-meshheading:1378932-Antibody Formation, pubmed-meshheading:1378932-Antibody Specificity, pubmed-meshheading:1378932-B-Lymphocytes, pubmed-meshheading:1378932-Chorionic Gonadotropin, pubmed-meshheading:1378932-Epitopes, pubmed-meshheading:1378932-Glycoprotein Hormones, alpha Subunit, pubmed-meshheading:1378932-Horses, pubmed-meshheading:1378932-Humans, pubmed-meshheading:1378932-Interleukin-2, pubmed-meshheading:1378932-Lymphocyte Activation, pubmed-meshheading:1378932-Macromolecular Substances, pubmed-meshheading:1378932-Mice, pubmed-meshheading:1378932-Molecular Sequence Data, pubmed-meshheading:1378932-Peptides, pubmed-meshheading:1378932-Sequence Alignment, pubmed-meshheading:1378932-Sheep, pubmed-meshheading:1378932-T-Lymphocytes
pubmed:articleTitle
Immune recognition of a molecule naturally presented as a monomeric or an oligomeric structure: the model of the human chorionic gonadotropin alpha subunit.
pubmed:affiliation
Laboratoire d'Immunologie, Faculté des Sciences Pharmaceutiques et Biologiques, Université René Descartes, CNRS, Paris, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't