Virusliterature

IV mutation literature information.

Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis.

PMID: 8879138 1996 Virus research

Abstract: Sequence analysis indicated that the unmapped mutation in the control of FM-MA virulence is either the K482-->R substitution in the PB2 protein or the D538-->G substitution in the PB1 protein.

Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino-Neu5Ac2en leads to instability of the enzyme.

PMID: 8918554 1996 Virology

Abstract: We previously isolated a variant of the influenza virus NWS/G70C, with a decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en in vitro, which has a mutation in one of the conserved residues of the neuraminidase Glu 119 to Gly.

Characterization of a hemagglutinin-specific inhibitor of influenza A virus.

PMID: 8941323 1996 Virology

Abstract: The resistant virus isolated contained a phenylalanine to serine change at amino acid 110 of the HA2 subunit.

Functional significance of varied quantitative and qualitative expression of HLA-A2.1 antigens in determining the susceptibility of cells to cytotoxic T lymphocytes.

PMID: 9157085 1996 Human immunology

Abstract: This difference results in an amino acid substitution from tyrosine to cysteine at position 99 of HLA-A2.1 heavy chains.

Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus.

PMID: 7605205 1995 Archives of virology

Abstract: Ts 412 has a single base substitution (G100-->A) leading to an amino acid replacement (Arg 25-->Lys) in the NS1 protein.

Abstract: Ts 451 also has a single base substitution (U273-->C) leading to an amino acid replacement (Ser 83-->Pro) in the NS1 protein.

Immunodominance with progenitor B cell diversity in the neutralizing antibody repertoire to influenza infection.

PMID: 7621857 1995 European journal of immunology

Abstract: A majority of mAb, established from individual BALB/c (H-2d) mice, select mutant viruses containing the same single amino acid substitution in the membrane distal ecto-domain, HA1 198 A-->E, whereas changes at either HA1 158 G-->E or HA1 198 A-->E are selected for by mAb from BALB.K (H-2k) donors.

Specific changes in the M1 protein during adaptation of influenza virus to mouse.

PMID: 7710364 1995 Archives of virology

Abstract: Comparison of the M gene sequences of the mouse brain adapted variants A/NWS/33 and A/WSN/33 to their parent, A/WS/33, identified two specific amino acid substitutions in the M1 protein which correlated with virulence for mouse: Ala41-->Val and Thr139-->Ala.

Genetic evidence for difference between intracellular and extracellular peptides in influenza A matrix peptide-specific CTL recognition.

PMID: 7822785 1995 Journal of immunology (Baltimore, Md.

Abstract: During the course of extensive mutagenesis of HLA-A2.1, we examined influenza A matrix peptide (FMP)-specific CTL recognition of HMy2.C1R (C1R) cells expressing mutant HLA-A2.1 molecules, sensitized with synthetic peptide, FMP 58-66, (exogenous peptide), or infected with influenza A virus (endogenous peptide).

Abstract: Pulse-chase analyses followed by endoglycosidase-H treatment show that the rate of maturation and processing of the five mutant HLA-A2 molecules in C1R cells is identical to that of wild type.

Abstract: The remaining three mutants, Y27N, Q32K, and S132C, fail to present exogenous peptide, but present endogenous peptide to FMP-specific CTL.

Abstract: Two of the five mutants, F9L an

Probing the structure of influenza B hemagglutinin using site-directed mutagenesis.

PMID: 7856092 1995 Virology

Abstract: None of the mutations affected hemagglutination activity, but mutations T196P or Q1971 eliminated binding of a monoclonal antibody.

Activation of the M2 ion channel of influenza virus: a role for the transmembrane domain histidine residue.

PMID: 8534806 1995 Biophysical journal

Abstract: Oocytes expressing the M2-H37E mutant protein also had a voltage-activated Cl- conductance that was observed only for oocytes that expressed a mass of protein exceeding a large threshold value.

Abstract: Oocytes expressing the M2-H37E protein also had a voltage-independent conductance with a current-voltage relationship similar to that of the wild-type M2 channel.

Abstract: Oocytes expressing the M2-H37G protein had a voltage-independent conductance with current-voltage relationship similar to that of the wild-type M2 channel.

Abstract: Oocytes expressing the M2-H37K and M2-

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