Abstract: Nucleotide sequence analysis revealed the presence of an intragenic mutation in each of the ts+ phenotypic revertant viruses, involving a substitution of valine for alanine at amino acid 23 of the NS1 protein.
Soluble HLA-A2.1 restricted peptides that are recognized by influenza virus specific cytotoxic T lymphocytes.
PMID: 1904085
1991
Journal of immunological methods
Abstract: Further substitution of threonine in position 65 with lysine resulted in a soluble antagonist peptide that inhibited sensitization.
Mutants and revertants of an avian influenza A virus with temperature-sensitive defects in the nucleoprotein and PB2.
Abstract: This ts defect is due to a single amino acid replacement (R162K) in a completely conserved region of the NP.
The 45 pocket of HLA-A2.1 plays a role in presentation of influenza virus matrix peptide and alloantigens.
PMID: 2026879
1991
Journal of immunology (Baltimore, Md.
Abstract: These mutants were transfected into HMy2.C1R cells and assessed for their ability to present influenza virus matrix M1 57-68 peptide and HTLV-I Tax-1 2-25 peptide to HLA-A2.1-restricted, peptide-specific CTL and to present alloantigens to HLA-A2-allospecific CTL lines.
Abstract: Thus, three single amino acid mutants were produced: 24A----S, 45 M----T, and 67V----S.
Single amino acid substitutions in the hemagglutinin can alter the host range and receptor binding properties of H1 strains of influenza A virus.
Abstract: Those with the mutant phenotype are unchanged at residue 129 but have a Gly to Glu substitution at residue 158, which is close to residue 129 on the HA1 subunit.
Abstract: We have previously characterized an influenza A (H1N1) virus which has host-dependent growth and receptor binding properties and have shown that a mutation which removes an oligosaccharide from the tip of the hemagglutinin (HA) by changing Asn-129 to Asp permits this virus to grow to high titer in MDBK cells, (C.
A dominant Th epitope in influenza nucleoprotein. Analysis of the fine specificity and functional repertoire of T cells recognizing a single determinant.
PMID: 1690775
1990
Journal of immunology (Baltimore, Md.
Abstract: The corresponding sequence of the NP of an equine influenza virus, A/Eq/Prague/56, which has a substitution (leucine to proline) at position 283, was not recognized by the lymph node cells from mice primed with either A/Okuda or A/Eq/Prague.
Mechanism of antigenic variation in an individual epitope on influenza virus N9 neuraminidase.
Abstract: A single mutation at residue 168 (Lys to Glu) in the H5 HA variants abolished CTL recognition; this same amino acid was shown previously to be critical for B-cell recognition (M.
Effect of a Tyr-to-His point-mutation at position 59 in the alpha-1 helix of the HLA-B27 class-I molecule on allospecific and virus-specific cytotoxic T-lymphocyte recognition.
PMID: 1701919
1990
Scandinavian journal of rheumatology. Supplement
Abstract: HLA-B2703, a mutation of HLA-B2705, is characterized by a Tyr-to-His substitution at position 59 in the alpha 1 domain of the class-I heavy chain.
Primary structure of the gene coding for the haemagglutinin of influenza virus A/Leningrad/385/80(H3N2): detection of a point mutation responsible for the antigenic drift.
Abstract: It was shown that a single mutation in an antigenic site (the change from isoleucine to leucine at position 51 of HA1 gene) caused an antigenic drift.
IV mutation literature information.
PMID: 
1991
Journal of virology
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