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 IV mutation literature information.


  Mutation of the alpha 2 domain disulfide bridge of the class I molecule HLA-A*0201. Effect on maturation and peptide presentation.
 PMID: 8071101       1994       Human immunology
Abstract: Mutant C164A cells infected with influenza virus were partially recognized by influenza matrix peptide-specific CTLs, while C101S cells were not lysed.
Abstract: Mutation of cysteine 101 to a serine (C101S) or of cysteine 164 to alanine (C164A) decreased the rate of maturation of the heavy chain, the total amount of mature heavy chain within the cell, and the level of surface expression.


  An estimation of the nucleotide substitution rate at defined positions in the influenza virus haemagglutinin gene.
 PMID: 8113760       1994       The Journal of general virology
Abstract: Particularly interesting amino acid changes, not previously reported, were observed in the p7 monoclonal antibody-specific mutants, in which only Gly to Ser and Gly to Asp at position 226 were detected.


  Attenuation of virulence in influenza B viral infection of volunteers.
 PMID: 8163832       1994       The Journal of infection
Abstract: A difference in MAb reactivity, together with an aspartate for asparagine amino acid substitution at position 196 in a 432 base pair region of the viral HA gene, was observed.


  Both major and minor peptide-binding pockets in HLA-A2 influence the presentation of influenza virus matrix peptide to cytotoxic T lymphocytes.
 PMID: 8183284       1994       Molecular immunology
Abstract: With the exception of Tyr substitution for Phe9, single amino acid substitutions in the peptide-binding groove had only minor effects on peptide binding.


  Affinity ranking of influenza neuraminidase mutants with monoclonal antibodies using an optical biosensor. Comparison with ELISA and slot blot assays.
 PMID: 8288899       1994       Journal of immunological methods
Abstract: Applications of this biosensor technique for comparing the binding of related neuraminidases, purified from escape mutants of influenza virus NWS/G70C/75 (N9), to two antibody Fab fragments, are described.


  Modulation of CD4+ T-cell recognition of influenza hemagglutinin by carbohydrate side chains located outside a T-cell determinant.
 PMID: 7685965       1993       Virology
Abstract: Two distinct T-cell clones raised to the H3 subtype influenza virus A/Memphis/71 fail to proliferate in response to other H3 viruses that contain the amino acid substitution Asp63-->Asn within the heavy (HA1) chain of the hemagglutinin (HA).


  Recognition by HLA-A2-restricted cytotoxic T lymphocytes of endogenously generated and exogenously provided synthetic peptide analogues of the influenza A virus matrix protein.
 PMID: 8300410       1993       Human immunology
Abstract: The endogenously presented analogues 58-66L60A, G61A, T65A, and L66A were recognized more efficiently than the corresponding exogenously presented analogues.
Abstract: This difference in recognition was most striking for peptide 58-66G61A.


  Influenza A virus haemagglutinin polymorphism: pleiotropic antigenic variants of A/Shanghai/11/87 (H3N2) virus selected as high yield reassortants.
 PMID: 8336120       1993       The Journal of general virology
Abstract: Differences in HA phenotype were related to a Ser to Ile change at amino acid position 186.


  A temperature-sensitive mutation in the acidic polymerase gene of an influenza A virus alters the regulation of viral protein synthesis.
 PMID: 8376958       1993       The Journal of general virology
Abstract: The temperature-sensitive defect of mutant ts 263 of fowl plague virus (FPV) is located in the acidic polymerase (PA) gene and is due to a single base substitution (C2036T), which leads to an amino acid replacement (Ala671 to Val) in a highly conserved region of the protein.


  Mutations in murine Mx1: effects on localization and antiviral activity.
 PMID: 8389079       1993       Virology
Abstract: These conclusions are based on the findings showing that: (i) none of the mutants retained antiviral activity; (ii) only a mutant with a Leu to Lys substitution at residue 612 within the nuclear targeting signal retained the characteristic punctate nuclear localization of wildtype Mx1; (iii) diffuse nuclear localization was observed for mutants with substitutions of Pro for Leu at residue 619, 626, or both 619 and 626, and deletions of residues 23 to 95, 159 to 185, 369 to 409, 387 to 440, 522 to 560, or 541 to 596; and (iv) cytoplasmic localization was observed for mutants with carboxy-terminal truncations of 15, 30, or 61 amino acids, or a deletion of residues 610 to 624.



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