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 IV mutation literature information.


  Mutations blocking the transport of the influenza virus hemagglutinin between the rough endoplasmic reticulum and the Golgi apparatus.
 PMID: 3024963       1986       The EMBO journal
Abstract: It involves the replacement of aspartic acid at position 457 by asparagine thereby introducing a new glycosylation site which appears to be located in a cryptic position in the lower part of the hemagglutinin stalk.
Abstract: The hemagglutinin of ts1 has an essential amino acid exchange at position 275 where serine is replaced by glycine.


  Primary structure of influenza virus genome regions coding for polypeptides from the major antigenic sites of H3 hemagglutinin.
 PMID: 3727394       1986       Virologie
Abstract: One of them was accompanied by a change in the coded amino acid (Asp53----Tyr) located in the antigenic site E of the HA glycoprotein.


  Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus.
 PMID: 3753607       1986       The Journal of cell biology
Abstract: Three mutants have been constructed that introduce single, nonconservative amino acid changes in the fusion peptide, and three fusion phenotypes were observed: substitution of glutamic acid for the glycine residue at the amino-terminus of HA2 abolished all fusion activity; substitution of glutamic acid for the glycine residue at position 4 in HA2 raised the threshold pH and decreased the efficiency of fusion; and, finally, extension of the hydrophobic stretch by replacement of the glutamic acid at position 11 with glycine yielded a mutant protein that induced fusion of erythrocytes with cells with the same efficiency and pH profile as the wild-type protein.


  Loss of enzyme activity in a site-directed mutant of influenza neuraminidase compared to expressed wild-type protein.
 PMID: 2417413       1986       Virology
Abstract: Full-length double-stranded DNA copies of the neuraminidase (NA) gene of influenza virus A/Tokyo/3/67 (N2) and a mutant generated in vitro by site-specific, oligonucleotide-directed mutagenesis with a substitution of leucine for tryptophan at position 178 were cloned into an SV40 late replacement expression vector.


  Conformational-dependent recognition of influenza virus hemagglutinin by murine T helper clones.
 PMID: 2420611       1986       European journal of immunology
Abstract: Five HA-specific Th clones failed to recognize X31 mutant viruses R19 and R20 each with a His to Arg substitution at position 17 of HA1.
Abstract: In addition, four of the five clones failed to recognize variant virus Eng-72 which has Arg to Gly substitution at position 208 in the interface antibody-binding region.


  Sequence of the neuraminidase gene of influenza virus A/Tokyo/3/67 and previously uncharacterized monoclonal variants.
 PMID: 6203216       1984       Virology
Abstract: In another variant, arginine at position 253 changed to serine, a change that also occurred in field strains.


  Characterization of the murine TH response to influenza virus hemagglutinin: evidence for three major specificities.
 PMID: 6208279       1984       Journal of immunology (Baltimore, Md.
Abstract: Three hybridomas with specificity 1 failed to respond to the PR8 mutant RV6 (Glu115----Lys), two with specificity 2 failed to respond to PR8 mutant DV4 (Ser136----Pro), and two with specificity 3 responded to all antibody-selected PR8 mutants without exception.


  Influenza virus site recognized by a murine helper T cell specific for H1 strains. Localization to a nine amino acid sequence in the hemagglutinin molecule.
 PMID: 6224879       1983       The Journal of experimental medicine
Abstract: A conserved region of the hemagglutinin molecule around amino acid position 115 in the heavy chain (HA1) was implicated as being important in this recognition by the lack of stimulatory activity associated with a glutamic acid to lysine substitution at position 115 in the laboratory mutant RV6, derived from wild-type PR8.


  Hemagglutinin of swine influenza virus: a single amino acid change pleiotropically affects viral antigenicity and replication.
 PMID: 6580621       1983       Proc Natl Acad Sci U S A
Abstract: Change at residue 155 from Gly to Glu is associated with change from L to H HA phenotype.



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