Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en.
Abstract: A variant of the influenza virus NWS/G70C has been generated which has decreased sensitivity in vitro to the neuraminidase-specific inhibitor, 4-guanidino-Neu5Ac2en.
Abstract: Sequence analysis of this virus revealed a mutation at a previously conserved site in the enzyme active site of the neuraminidase, Glu 119 to Gly.
Identification of the sites for suppressor mutations on the hemagglutinin molecule to temperature-sensitive phenotype of the influenza virus.
Abstract: Nucleotide 28 mutated from T to C which leads to a change of amino acid 3 from Leu to Phe.
Role of GTPase activity of murine Mx1 protein in nuclear localization and anti-influenza virus activity.
PMID: 9049394
1995
The Journal of general virology
Abstract: Mutant S50I, which had no GTP-binding or GTPase activities, formed linear structures in nuclei and lacked anti-viral activity, while C71S appeared diffuse in nuclei as minute dots without granules, but retained the inhibitory activity against influenza virus growth.
Abstract: Wild-type Mx1 and two mutant Mx1 proteins, each carrying a single mutation either in the GTP-binding motif (S50I) or in the self-assembly motif (C71S), were expressed in MDCK cells.
Stoichiometry of recombinant cystic fibrosis transmembrane conductance regulator in epithelial cells and its functional reconstitution into cells in vitro.
PMID: 7507932
1994
The Journal of biological chemistry
Abstract: Furthermore, expression of the most frequent mutant allele of the cystic fibrosis (CF) gene, the delta F508 mutant in these epithelial cells, indicated that it is biosynthetically arrested at the endoplasmic reticulum and fails to traffic to the plasma membrane.
Influenza A virus M2 ion channel protein: a structure-function analysis.
Abstract: A glycosylated M2 mutant protein (M2 + V, A30T) exhibited an ion channel activity with a voltage-activated, time-dependent kinetic component.
Abstract: The membrane currents of oocytes expressing mutant M2 ion channels were measured at both normal and low pH, and the amantadine-resistant mutant containing the change of alanine at residue 30 to threonine was found to have a significantly attenuated low pH activation response.
Neutralization escape mutants of type A influenza virus are readily selected by antisera from mice immunized with whole virus: a possible mechanism for antigenic drift.
PMID: 7527838
1994
The Journal of general virology
Abstract: The HA genes of three of these were part sequenced and had a predicted single amino acid substitution (Gly-144-->Glu) in site A.
The small GTP-binding protein rab6 functions in intra-Golgi transport.
Abstract: Over-expression of wild-type rab6 and rab6 Q72L greatly reduced transport of both markers between cis/medial (alpha-mannosidase II positive) and late (sialyl-transferase positive) Golgi compartments, without affecting transport from the endoplasmic reticulum (ER) to cis/medial-Golgi or from the trans-Golgi network (TGN) to the plasma membrane.
Abstract: Overexpression of both rab6 Q72L and rab6 T27N altered the morphology of the Golgi apparatus as well as that of the TGN, as assessed at the immunofluorescence level with several markers.
Abstract: We have transiently overexpressed in mouse L cells and human HeLa cells wild-type rab6, GTP (rab6 Q72L), and GDP (rab6 T27N) -bound mutants of rab6 and analyzed the intracellular transport of a soluble secreted form of alkaline phosphatase (SEAP) and of a plasma
[Changes in its hemagglutinin during the adaptation of the influenza virus to mice and their role in the acquisition of virulent properties and resistance to serum inhibitors].
Abstract: In another experiment, the adapted virus (15th passage) did not differ in its antigenic, virulent, and reproductive properties from clone 7p but had only one substitution in HA Asn127-->Asp.
Abstract: Passages of influenza A/USSR/90/77 virus in mouse lungs produced a virulent virus (18th passage) carrying two mutations in hemagglutinin (HA) Asn127-->Asp and Tre89-->Ala.
Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation.
IV mutation literature information.
PMID: 
1995
Virology
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