Linked Life Data

8765034

Source:http://linkedlifedata.com/resource/pubmed/id/8765034

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1996-10-24
pubmed:abstractText
Antigen presentation to CD8+ cytotoxic T lymphocytes (CTL) usually involves proteolytic cleavage of antigen in the cytosol and the delivery of epitope peptides onto major histocompatibility complex class I molecules in the endoplasmic reticulum (ER) via the heterodimeric peptide transporter TAP1/TAP2. In the few exceptional cases where TAP-independent presentation of an endogenously expressed protein has been observed, the epitope-containing domain of the protein either has naturally accessed or has been directed into the ER lumen where it is thought to become susceptible to ER proteases. Here, we describe a novel example of TAP-independent processing involving the Epstein-Barr virus (EBV) latent membrane protein LMP2, a multiple membrane-spanning protein with minimal projection into the ER. Expression of LMP2 in the TAP-T2 cell line, whether from the resident EBV genome or from a recombinant vaccinia virus vector vacc-LMP2, rendered the cells sensitive to recognition by CTL clones specific for two HLA-A2.1-restricted peptide epitopes, LMP2 329-337 or 426-434. Vacc-LMP2-mediated sensitization to lysis required expression of the antigen de novo in T2 cells and was blocked by brefeldin A. In the same experiments, two other EBV-specific CTL epitopes, one derived from LMP2 but restricted through a different HLA allele (A11), the other restricted through A2.1 but derived from a different viral protein (BMLF1), did not display TAP-independent processing. The results are discussed in relation to the unusual topology of LMP2 in the membrane and the position of the epitope peptides within that structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1875-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8765034-ATP-Binding Cassette Transporters, pubmed-meshheading:8765034-Amino Acid Sequence, pubmed-meshheading:8765034-Antigen Presentation, pubmed-meshheading:8765034-Antigens, Viral, pubmed-meshheading:8765034-Burkitt Lymphoma, pubmed-meshheading:8765034-Cell Line, Transformed, pubmed-meshheading:8765034-Epitopes, pubmed-meshheading:8765034-Genetic Vectors, pubmed-meshheading:8765034-HLA-A2 Antigen, pubmed-meshheading:8765034-Herpesvirus 4, Human, pubmed-meshheading:8765034-Humans, pubmed-meshheading:8765034-Membrane Proteins, pubmed-meshheading:8765034-Molecular Sequence Data, pubmed-meshheading:8765034-T-Lymphocytes, Cytotoxic, pubmed-meshheading:8765034-Tumor Cells, Cultured, pubmed-meshheading:8765034-Vaccinia virus, pubmed-meshheading:8765034-Viral Matrix Proteins
pubmed:year
1996
pubmed:articleTitle
Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2.
pubmed:affiliation
CRC Institute for Cancer Studies, University of Birmingham, GB.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't