Abstract: This results in a substitution of isoleucine for leucine at amino acid position 512 in the cap-binding protein, PB2.
The kinetics of peptide binding to HLA-A2 and the conformation of the peptide-A2 complex can be determined by amino acid side chains on the floor of the peptide binding groove.
Abstract: HLA-A2 molecules with naturally occurring single amino acid substitutions of Phe to Tyr at position 9 (HLA-A2.4a, Tyr9) and Tyr to Cys at position 99 (HLA-A2.4b, Cys99) and a site directed mutant with a Val to Leu substitution at position 95 (Leu95) were examined for their ability to present the influenza virus matrix M1 55-73 peptide and several sequence variants of the M1 peptide to a panel of 36 M1 55-73-specific HLA-A2.1-restricted CTL lines.
The structure of a membrane fusion mutant of the influenza virus haemagglutinin.
Abstract: We have determined the neutral pH crystal structure of one such mutant, HA2 112 Asp----Gly.
Single-amino-acid substitution in an antigenic site of influenza virus hemagglutinin can alter the specificity of binding to cell membrane-associated gangliosides.
Abstract: The majority of variants, including one with a substitution near the receptor-binding site (Asn-133----Lys), did not differ from the parent in specificity for receptor molecules.
Two murine natural polyreactive autoantibodies are encoded by nonmutated germ-line genes.
Abstract: Compared with the germ-line VH 1210.7 gene, E7 has a single nucleotide difference leading to a silent mutation at position 15, whereas D23 seems to be encoded by germ-line VH 101 with one nucleotide difference causing replacement of Ser-84 by Ala.
[Antigenic variability of avian influenza virus A/H13, isolated in the USSR].
Abstract: Two replacements of arginine by lysine and asparagine by serine in positions 15 and 16, respectively, are the most significant.
Class II-restricted T-cell clones to a synthetic peptide of influenza virus hemagglutinin differ in their fine specificities and in the ability to respond to virus.
Abstract: The response of the clones to peptide analogs identified certain residues within the sites that were critical for recognition, with the substitution Gln-311----Ser having a differential effect on clones responding to the N-terminal site.
Fine specificity of murine class II-restricted T cell clones for synthetic peptides of influenza virus hemagglutinin. Heterogeneity of antigen interaction with the T cell and the Ia molecule.
PMID: 2453566
1988
Journal of immunology (Baltimore, Md.
Abstract: Peptide analogs or mutant viruses with a single amino acid substitution at position 63 (Asp to Asn or Tyr) reduced the responses of the T cell clones to variable extents, suggesting that Asp63 may form part of overlapping T cell determinants.
Amino acid substitution at position 226 of the hemagglutinin molecule of influenza (H1N1) virus affects receptor binding activity but not fusion activity.
Abstract: Two mutant HA proteins containing single amino acid substitutions of Asn and Met for Gln at position 226 retained their receptor binding activity, but others with amino acid substitutions Glu, His, Leu, Val, and Thr for Gln at position 226 lost this activity.
A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits.
Abstract: However, one of these mutations, substituting tyrosine for cysteine at amino acid 543, changed HA from a protein that was endocytosed at a very low rate to a protein that readily entered coated pits, was internalized, and apparently recycled to the cell surface.
IV mutation literature information.
PMID: 
1990
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