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Three T-cell epitopes within the C-terminal 265 amino acids of the matrix protein pp65 of human cytomegalovirus recognized by human lymphocytes.
- Source :
-
Journal of medical virology [J Med Virol] 1997 May; Vol. 52 (1), pp. 68-76. - Publication Year :
- 1997
-
Abstract
- Although a T-cell response in human cytomegalovirus (HCMV)-immune individuals exists against the most abundantly expressed protein pp65 of the virus matrix, less is known about the determinants that evoke this response. The aim of the study was to identify regions within HCMV pp65 (ppUL83) that contain sequences for the cellular immune response by the use of three recombinant overlapping beta-galactosidase pp65 fusion proteins (C74, C35, and C47), covering the C-terminal 265 amino acids of the entire pp65 sequence. Two T-cell epitope determinants were recognized by human lymphocytes of healthy, HCMV-seropositive, human leukocyte antigen (HLA)-typed individuals. One T-cell determinant (amino acids [aa] 303-388) was localized in the mid-region of the entire pp65 sequence and a second T-cell determinant (aa 477-561) within the C-terminal region. By fine mapping with synthetic hexadecamer peptides three T-cell epitopes were identified within these two regions: P10-I (aa 361-376) in the mid-region, P3-II (aa 485-499), and P6-II (aa 509-524) in the C-terminal region. Inhibition studies with monoclonal antibodies to HLA class I or class II revealed a class II restricted response to peptides P10-I or P6-II, respectively. P10-I responders shared the HLA-DR11 allele and P6-II responders the -DR3 allele. Therefore, these T-cell epitopes of HCMV pp65 might be presented in association with particular HLA class II alleles.
- Subjects :
- Alleles
Amino Acid Sequence
Cell Line
Cytomegalovirus chemistry
Epitope Mapping
Epitopes, T-Lymphocyte biosynthesis
Epitopes, T-Lymphocyte chemistry
HLA-DR Antigens immunology
HLA-DR Antigens metabolism
Humans
Lymphocyte Activation drug effects
Molecular Sequence Data
Peptide Fragments immunology
Peptide Fragments metabolism
Peptide Fragments pharmacology
Phosphoproteins chemistry
Recombinant Fusion Proteins immunology
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins metabolism
Viral Matrix Proteins chemistry
Cytomegalovirus genetics
Cytomegalovirus immunology
Epitopes, T-Lymphocyte immunology
Phosphoproteins immunology
Phosphoproteins metabolism
Viral Matrix Proteins immunology
Viral Matrix Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0146-6615
- Volume :
- 52
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of medical virology
- Publication Type :
- Academic Journal
- Accession number :
- 9131460
- Full Text :
- https://doi.org/10.1002/(sici)1096-9071(199705)52:1<68::aid-jmv11>3.0.co;2-x