Virusliterature

IV mutation literature information.

[Changes in the amino acid sequence of hemagglutinin during sequential adaptation of human influenza virus A to replication in mice].

PMID: 3211187 1988 Molekuliarnaia genetika, mikrobiologiia i virusologiia

Abstract: At the first stage of adaptation (3-rd passage) only a single mutation was detected: Asn 127----Asp.

Abstract: In the HA1 coding region of mice-adapted virus (11 passages) there are two amino acid substitutions: Thr 89----Ala and Asn 127----Asp.

A mutation in the PA protein gene of cold-adapted B/Ann Arbor/1/66 influenza virus associated with reversion of temperature sensitivity and attenuated virulence.

PMID: 3354203 1988 Virology

Abstract: The predicted PA proteins of wt and ca B/AA/1/66 are known to differ by six amino acid substitutions including a valine to methionine substitution at residue 431.

Structure of an escape mutant of glycoprotein N2 neuraminidase of influenza virus A/Tokyo/3/67 at 3 A.

PMID: 3379640 1988 Journal of molecular biology

Abstract: The mutant virus, selected by growing the virus in the presence of a monoclonal antibody to the neuraminidase, is shown to have undergone a single amino acid change of lysine to glutamic acid at residue 368.

Extragenic and intragenic suppression of a transport mutation in the hemagglutinin gene of an influenza A virus as revealed by backcross and sequence determination.

PMID: 3576971 1987 Virology

Abstract: The amino acid replacement in position 480 from Thr to Ile, leading to the loss of a complex carbohydrate side chain, is responsible for the ts phenotype.

Crystals of antibodies complexed with influenza virus neuraminidase show isosteric binding of antibody to wild-type and variant antigens.

PMID: 3811232 1987 Virology

Abstract: Crystals have been grown of Fab fragments of monoclonal antibody NC41, complexed with influenza virus neuraminidase (NA) of the N9 subtype and with a variant of N9 NA having a sequence change of Asn to Asp at position 331.

Abstract: This reduces, but does not abolish, the binding of NC41 antibody (in the case of another variant, Ser 371 to Leu, binding of NC41 antibody appears to be abolished).

Effects of site-specific mutation on structure and activity of influenza virus B/Lee/40 neuraminidase.

PMID: 3811237 1987 Virology

Abstract: Mutation of Trp 364 to Leu abolished detectable enzyme activity, while mutation of Thr 368 to Val reduced enzyme activity to less than 25% of wild-type levels.

Abstract: Mutation of an apparently unpaired cysteine residue to serine at position 251 had no effect on protein transport or folding as judged by cell-surface reactivity with monoclonal antibodies, and the NA retained enzyme activity, confirming that this Cys is not essential for correct folding of the polypeptide.

Mutational analysis of the signal-anchor domain of influenza virus neuraminidase.

PMID: 3025850 1987 Proc Natl Acad Sci U S A

Abstract: On the other hand, substitution of arginine for isoleucine at position 26 blocked the migration of the NA protein from the Golgi complex to the cell surface.

Abstract: When the altered NA proteins were expressed in CV-1 cells, two phenotypes were observed: substitution of arginine in place of glycine at position 11 and substitution of aspartic acid for valine at position 17 did not abolish the signal, the anchor, or the transport functions.

[Expression and mutagenesis of genes coding for protein synthesis in the influenza virus].

PMID: 3033905 1987 Voprosy virusologii

Abstract: Double-stranded cDNA copies of the neuraminidase genes of influenza viruses A/Tokyo/3/67 (N2), A/tern/Australia/G70C/75 (N9), and B/Lee/40, and the hemagglutinin genes of A/Memphis/1/71 (H3) and B/Hong Kong/8/73 were cloned into a SV40 vector in which the late region was replaced by the influenza sequences.

Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane.

PMID: 3038931 1987 The Journal of cell biology

Abstract: Eight mutant proteins were also examined: dTM14, lacking six amino acids from the transmembrane domain; TA2, lacking an oligosaccharide in the extracellular domain; QN2, possessing an extra N-linked oligosaccharide in the extracellular domain; CS2, possessing a serine instead of a cysteine at residue 489 in the cytoplasmic domain, preventing palmitate addition to the glycoprotein; TMR-stop, lacking the entire cytoplasmic domain except an arginine at residue 483; and three chimeric proteins, G mu, G23, and GHA, containing in place of the 29 amino acid wild type cytoplasmic domain the cytoplasmic domains from the surface IgM from the spike protein of the infectious bronchitis virus or from the hemagglutinin protein of the influenza virus, respectively.

Variant influenza virus hemagglutinin that induces fusion at elevated pH.

PMID: 3003392 1986 Journal of virology

Abstract: This substitution, asparagine for aspartic acid at position 132, disrupted a highly conserved interchain salt bridge between adjacent HA2 subunits.

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