literature

IV mutation literature information.

Sensitive Detection and Simultaneous Discrimination of Influenza A and B Viruses in Nasopharyngeal Swabs in a Single Assay Using Next-Generation Sequencing-Based Diagnostics.

PMID: 27658193 2016 PloS one

Abstract: Of the influenza A viruses, 66.7% of A(H3N2) viruses tested had a E627K mutation in the PB2 protein, and 87.8% of the influenza A viruses contained the S31N mutation in the M2 protein.

Discussion: A mutation of PB2 E627K has been reported to confer high virulence to the virus by enhancing replication efficiency, and increasing polymerase activity and disease severity of avian influenza viruses in mammals.

Discussion: Sequence analysis of 123 influenza A viruses revealed that 66.7%(82/123) of A(H3N2) viruses had a single signature mutation of E627K in the PB2 protein, and 88%(108/123) of influenza A(H3N2 and pdH1N1) viruses contained the S31N mutation in

Amino acid substitutions involved in the adaptation of a novel highly pathogenic H5N2 avian influenza virus in mice.

PMID: 27663652 2016 Virology journal

1Abstract: FINDINGS: Amino acid changes were identified in the MA-DK19 PB2 (E627K), PB1 (

Result: In this study, amino acid substitutions, in the PB2 (E627K), PB1 (I181T), HA (A150S), NS1 (WRNKVAD was extended at the C-terminal of the protein), and NS2 (E69G) proteins were identified in a MA-6DK19.

Result: The E627K substitution in the PB2 protein has been reported to influence host range and to confer increased virulence in models of H3, H5, H6, and H9 infection.

Adaptive amino acid substitutions enhance the virulence of a reassortant H7N1 avian influenza virus isolated from wild waterfowl in mice.

PMID: 25555151 2015 Virology

Abstract: Analysis of the variant virus genomes revealed amino acid changes in the PB2 (E627K), HA (H3 numbering; E114K, G205E, and G218E), and NA (S350N) proteins.

V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.

PMID: 25641917 2015 Proteomics

Abstract: In this study, sp-A as a potential virulence determinant associated H9N2 AIV PB2 E627K mutation was identified using comparative proteomics.

PB2 segment promotes high-pathogenicity of H5N1 avian influenza viruses in mice.

PMID: 25713566 2015 Frontiers in microbiology

Discussion: Mutation of Glu 627Lys or 701Asn in PB2 increases the pathogenesis of viruses in mammalian hosts (Li et al.,; de Jong et al.,) and transmissibility between mammalian models (Gabriel et al.,; Gao et al.,; Steel et al.,).

Adaptive amino acid substitutions enhance the virulence of an H7N7 avian influenza virus isolated from wild waterfowl in mice.

PMID: 25769645 2015 Veterinary microbiology

Abstract: Genomic analysis of the adapted variant viruses revealed amino acid changes in the PB2 (E627K), PB1 (R118I), PA (L550M), HA (G214R), and NA (S372N) proteins.

V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.

PMID: 25782865 2015 Archives of virology

Abstract: Polymerase complexes possessing PB2-E627K displayed 16.1-fold higher viral polymerase activity when compared to the wild-type virus, which may account for enhanced virulence of this virus.

Abstract: The PB2-E627K substitution rapidly appeared at the second passage and played a decisive role in virulence.

Molecular characterization of mammalian-adapted Korean-type avian H9N2 virus and evaluation of its virulence in mice.

PMID: 26224460 2015 Journal of microbiology (Seoul, Korea)

Abstract: Moreover, reverse genetic studies established that an E627K substitution in PB2 and the loss of the N-glycosylation site in the HA protein (aa166) are critical virulence markers in the mouse-adapted H9N2 virus.

V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.

PMID: 26391278 2015 Scientific reports

Introduction: As residues at positions 627 and 701 of the polymerase basic protein 2 (PB2) are considered critical for the mammalian adaptation of avian influenza viruses, several studies have independently shown that single E627K (glutamic acid to lysine) or D701N (aspartic acid to asparagine) mutations could increase polymerase activity and viral replication in mammalian cells and the pathogenicity of H7N9 viruses in the BALB/c mouse model.

Introduction: Our findings show that both the E627K and D701N mutations occurred in ferrets that had direct contact with infected animals within a few days post-exposure.

Introduction: Yet it is still unknown whether spontaneous emergence of dual D701N and E627K mutations can occur readily in infecte

Influenza A(H6N1) Virus in Dogs, Taiwan.

PMID: 26583707 2015 Emerging infectious diseases

Abstract: Molecular analysis indicated that this isolate was closely related to influenza A(H6N1) viruses circulating in Taiwan and harbored the E627K substitution in the polymerase basic 2 protein, which indicated its ability to replicate in mammalian species.

Method: Other major signatures associated with replication ability in a mammalian host or pathogenicity were also observed, including E627K in the PB2 and the PDZ ligand domain at the C-terminal region of NS1 of this virus.

Table: E627K

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