IV mutation literature information.


  A reverse genetics approach for recovery of recombinant influenza B viruses entirely from cDNA.
 PMID: 12388735       2002       Journal of virology
Abstract: We adapted the technique for engineering influenza B virus and generated a mutant bearing an amino acid change E116G in the viral neuraminidase which was resistant in vitro to the neuraminidase inhibitor zanamivir.


  A nontoxic chimeric enterotoxin adjuvant induces protective immunity in both mucosal and systemic compartments with reduced IgE antibodies.
 PMID: 12402195       2002       The Journal of infectious diseases
Abstract: A novel nontoxic form of chimeric mucosal adjuvant that combines the A subunit of mutant cholera toxin E112K with the pentameric B subunit of heat-labile enterotoxin from enterotoxigenic Escherichia coli was constructed by use of the Brevibacillus choshinensis expression system (mCTA/LTB).


  Mechanism by which mutations at his274 alter sensitivity of influenza a virus n1 neuraminidase to oseltamivir carboxylate and zanamivir.
 PMID: 12435681       2002       Antimicrobial agents and chemotherapy
Abstract: An influenza A/H1N1 variant selected in vitro with reduced susceptibility to oseltamivir carboxylate contains a His274Tyr mutation.
Abstract: Interestingly, His274Asn, as well as His274Gly, His274Ser, and His274Gln, also displayed reduced sensitivity to zanamivir and its analogue, 4-amino-Neu5Ac2en.
Abstract: Loss of this slow-binding inhibition in the His274Tyr and His274Phe mutant NA but not in His274Asn, His274Gly, His274Ser, or His274Gln supports the conclusion that the conformational change of Glu276 is restricted in the  PMID: 12438632       2002       Journal of virology
Abstract: In contrast, deletion of RKLKR or substitution of Lys with Asn at position 102 or 104 of RKLKR resulted in a lethal mutation.
Abstract: Substitution of Arg with Ser at position 101 or 105 of RKLKR did not have a major impact on nuclear export of RNP or viral replication.


  Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation.
 PMID: 11159448       2001       Biophysical journal
Abstract: Cells expressing wild-type influenza virus hemagglutinin (HA) or HA with a point mutation within the transmembrane domain (G520L) were bound to red blood cells and exposed to low pH for short times at suboptimal temperatures followed by reneutralization.
Abstract: For both HA and G520L, the extents of fusion did not depend on the temperature at which pH was lowered, but fusion from the intermediate was extremely sensitive to the temperature to which the cells were raised.
Abstract: In contrast, generating intermediates in the same way with G520L yielded kinetics of fusion that did not depend on the time intermediates were maintained after reneutralization.


  Selection of influenza virus mutants in experimentally infected volunteers treated with oseltamivir.
 PMID: 11170976       2001       The Journal of infectious diseases
Abstract: They bore a substitution His274Tyr in the NA.


  An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells.
 PMID: 11408592       2001       Molecular biology of the cell
Abstract: Ultrastructural analysis indicated that compared with MAL bearing an intact RWKSS sequence, a mutant with lysine -3 substituted by serine showed a twofold increased presence in clathrin-coated cytoplasmic structures and a reduced expression on the plasma membrane.


  A single amino acid alteration in the human parainfluenza virus type 3 hemagglutinin-neuraminidase glycoprotein confers resistance to the inhibitory effects of zanamivir on receptor binding and neuraminidase activity.
 PMID: 11413297       2001       Journal of virology
Abstract: ZM1 exhibited a markedly fusogenic plaque morphology and harbored two HN gene mutations resulting in two amino acid alterations, T193I and I567V.


  [Reduction of the functional match of influenza virus hemagglutinin and neuraminidase after reassortation of genes].
 PMID: 11443933       2001       Molekuliarnaia biologiia
Abstract: Amino acid substitution K156E, which increases a negative charge at the edge of the receptor-binding pocket of HA large subunit (HA1), was revealed in two independent variants.


  Diverged evolution of recent equine-2 influenza (H3N8) viruses in the Western Hemisphere.
 PMID: 11504416       2001       Archives of virology
Abstract: This low evolution rate was probably due to a unique alternating Ser138 to Ala138 substitutions at antigenic site A.



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