ViMRT
}  
 
Home   
< Docs   

 IV mutation literature information.


  A single amino acid change in the C-terminal domain of the matrix protein M1 of influenza B virus confers mouse adaptation and virulence.
 PMID: 15892972       2005       Virology
Abstract: Sequencing and characterization of intermediate passages suggested that one change in the C-terminal domain of the M1 protein, an asparagine to a serine at position 221, was responsible for acquisition of virulence and lethality.


  Full restoration of viral fitness by multiple compensatory co-mutations in the nucleoprotein of influenza A virus cytotoxic T-lymphocyte escape mutants.
 PMID: 15914859       2005       The Journal of general virology
Abstract: Here, the effect on viral fitness of four other co-mutations associated with R384G was investigated by using plasmid-driven rescue of mutant viruses.
Abstract: One of these is the arginine-to-glycine substitution at position 384 (R384G).
Abstract: This substitution alone, however, is detrimental to viral fitness, which is overcome in part by the functionally compensating co-mutation E375G.
Abstract: Whilst none of these alternative co-mutations alone compensated functionally for the detrimental effect of the R384G substitution, the M239V substitution improved viral fitness of viruses containing 375G and 384R.


  Variation of the conserved neutralizing epitope in influenza B virus victoria group isolates in Japan.
 PMID: 16081981       2005       Journal of clinical microbiology
1Abstract: Amino acid substitutions (D164E or N165K) were observed at the ""tip"", and the epitope was altered."


  Molecular basis of replication of duck H5N1 influenza viruses in a mammalian mouse model.
 PMID: 16140781       2005       Journal of virology
Abstract: A single amino acid substitution (Asp to Asn) at position 701 of PB2 enabled DKGX/22 to infect and become lethal for mice.
Abstract: We find that the PA, NA, and NS genes of DKGX/22 could attenuate DKGX/35 virus to some extent, but PB2 of DKGX/22 virus attenuated the DKGX/35 virus dramatically, and an Asn-to-Asp substitution at position 701 of PB2 plays a key role in this function.


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 16140782       2005       Journal of virology
1Abstract: G1S forms a V with a disrupted ""glycine edge"" on its N-terminal arm and G1V adopts a slightly tilted linear helical structure in membranes."
Abstract: Abolishment of the kink in G1V results in reduced hydrophobic penetration of the lipid bilayer and an increased propensity to form beta-structures at the membrane surface.
Abstract: The most N-terminal residue of this domain, a glycine, is highly conserved and is particularly critical for HA function; G1S and G1V mutant HAs cause hemifusion and abolish fusion, respectively.
Abstract: We have determined the atomic resolution structures of the G1S and G1V mutant fusion domains in membrane environments.


  Neuraminidase inhibitor-resistant influenza viruses may differ substantially in fitness and transmissibility.
 PMID: 16189083       2005       Antimicrobial agents and chemotherapy
Abstract: Both mutants showed decreased sensitivity to oseltamivir carboxylate, and the RG R292K-NA virus showed cross-resistance to zanamivir.
Abstract: The R292K mutation caused greater reduction of sialidase activity and thermostability than the E119V mutation.
Abstract: The NA defect caused by the R292K mutation was associated with compromised growth and transmissibility, whereas the growth and transmissibility of the RG E119V-NA virus were comparable to those of RG WT virus.
Abstract: We generated recombinant viruses containing either the wild-type NA (RG WT virus) or a single amino acid change at NA residue 119 (RG


  Polymer-bound 6' sialyl-N-acetyllactosamine protects mice infected by influenza virus.
 PMID: 16214231       2005       Antiviral research
Abstract: Sequencing of the HA gene of the mouse-adapted virus A/NIB/23/89-MA revealed a loss of the glycosylation sites in positions 94 and 163 of HA1 and substitutions 275Asp-->Gly in HA1 and 145Asn-->Asp in HA2.


  Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.
 PMID: 16227287       2005       Journal of virology
Abstract: Additionally, a reassortant of strain A/WSN/33 (WSN), containing the Ud HA gene with mutations C555S, C562S, and C565S, produced virus that could form plaques on regular MDCK cells and had only moderately decreased replication, suggesting differences in the interactions between Ud and WSN HA and internal viral proteins.
Abstract: Mutant viruses containing HA-C562S and HA-C565S mutations had reduced growth and failed to form plaques in MDCK cells but formed wild-type-like plaques in an MDCK cell line expressing wild-type HA.


  Genetic analysis of influenza virus NS1 gene: a temperature-sensitive mutant shows defective formation of virus particles.
 PMID: 16306596       2005       Journal of virology
Abstract: Mutant 11C contained three mutations that led to amino acid exchanges, V18A, R44K, and S195P, all of which were required for the ts phenotype, and was characterized further.


  [Antigenic and genetic study of hemagglutinin gene of influenza virus (H3N2) circulated in China in 2004].
 PMID: 16415996       2005       Zhonghua shi yan he lin chuang bing du xue za zhi
Abstract: There were four important mutant positions, they were 159 Y>F, 189 S>N, 145 K>N, 226 V>I, respectively.



Browser Board

 Co-occurred Entities




   Filtrator