PMID- 7678302
OWN - NLM
STAT- MEDLINE
DCOM- 19930211
LR  - 20200724
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 67
IP  - 2
DP  - 1993 Feb
TI  - Immunodominant T-cell epitopes of rubella virus structural proteins defined by 
      synthetic peptides.
PG  - 673-81
AB  - Sets of overlapping synthetic peptides containing predicted T-cell epitope motifs 
      were designed from the murine monoclonal antibody-defined map of linear B-cell 
      epitope domains within each of the structural proteins of rubella virus (RV). The 
      peptides represented well-defined subsequences of two capsid domains (C1 to C29 
      and C64 to C97), of a domain of glycoprotein E1 containing neutralizing 
      determinants (E1(202) to E1(283), and of a domain of glycoprotein E2 (E2(31) to 
      E2(105). With the exception of peptides representing C64 to C97, each set of 
      peptides stimulated varied but individually specific lymphoproliferative 
      responses in peripheral blood mononuclear cells from 25 to 50% of a 
      representatively large number of normal, RV-immune human donors with diverse 
      human leukocyte antigen (HLA) backgrounds. Responses were mediated by CD4+ T 
      cells in association with HLA class II antigens, though lymphoproliferative 
      responses to a given peptide were usually not HLA-DR allele specific. Correlation 
      analysis of responses to overlapping peptides suggests that there is an 
      immunodominant T-proliferative epitope within C14 to C29 recognized by 
      approximately 50% of the donor population. However, limiting-dilution analysis 
      indicated much variability between individuals in lymphocyte recognition of this 
      T-cell determinant, even within similar HLA-DR contexts. Thus, the fine 
      specificity of relatively immunodominant T-cell epitopes may vary from individual 
      to individual. Synthetic peptides with predicted T-cell motifs have proved to be 
      useful probes of the molecular determinants of cellular immunity to RV and should 
      expand the rational basis for the design of synthetic RV vaccines.
FAU - McCarthy, M
AU  - McCarthy M
AD  - Department of Neurology, University of Texas Health Science Center, Houston 
      77225.
FAU - Lovett, A
AU  - Lovett A
FAU - Kerman, R H
AU  - Kerman RH
FAU - Overstreet, A
AU  - Overstreet A
FAU - Wolinsky, J S
AU  - Wolinsky JS
LA  - eng
GR  - AI26943/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Viral)
RN  - 0 (Epitopes)
RN  - 0 (Peptide Fragments)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (Viral Structural Proteins)
RN  - 131016-03-0 (E2 envelope protein, Rubella virus)
SB  - IM
EIN - J Virol 1993 Apr;67(4):2426
MH  - Amino Acid Sequence
MH  - Antibodies, Monoclonal
MH  - Antibodies, Viral/blood/immunology
MH  - Capsid/immunology
MH  - Epitopes/*immunology
MH  - Humans
MH  - Lymphocyte Activation/immunology
MH  - Major Histocompatibility Complex
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemical synthesis/*immunology
MH  - Rubella/immunology
MH  - Rubella virus/*immunology
MH  - T-Lymphocytes/*immunology
MH  - Viral Envelope Proteins/immunology
MH  - Viral Structural Proteins/*immunology
PMC - PMC237418
EDAT- 1993/02/01 00:00
MHDA- 1993/02/01 00:01
PMCR- 1993/02/01
CRDT- 1993/02/01 00:00
PHST- 1993/02/01 00:00 [pubmed]
PHST- 1993/02/01 00:01 [medline]
PHST- 1993/02/01 00:00 [entrez]
PHST- 1993/02/01 00:00 [pmc-release]
AID - 10.1128/JVI.67.2.673-681.1993 [doi]
PST - ppublish
SO  - J Virol. 1993 Feb;67(2):673-81. doi: 10.1128/JVI.67.2.673-681.1993.