Abstract: Mutations in PB2 (E627K), PB2 (K683T), PB1-F2 (N47S), HA (N283D), HA(K321E), NA(A137V), NA(K296R) and M2 (C19Y) were identified in the human isolate while no mutations were found in PB1, Discussion: Second, E627K in PB2 of the human H7N4 virus may have been a determinant of host range.
Effect of the selection pressure of vaccine antibodies on evolution of H9N2 avian influenza virus in chickens.
Discussion: Mutation on the RNP complex will increase the infectivity and host range of influenza viruses, such as 588V, E627K, G685R and D701N on PB2 (Song et al.; Wei and Liu; Xiao et al.; Zhang et al.).
Genetic and antigenic characterization of influenza A/H5N1 viruses isolated from patients in Indonesia, 2008-2015.
Result: Both PB2-E627K (5 of 35 viruses) and PB2-D701N (1 virus) substitutions were observed in a limited number of the novel viruses presented in this study.
Result: In particular, PB2-E627K is a key molecular determinant of host range and a virulence factor during human infection with
Discussion: Although some genetic diversity was observed in the polymerase genes, well-known substitutions such as PB2-E627K and PB2-D701N, which are often selected upon infection of humans and affects the virulence of avian influenza viruses such as H5N1, were not commonly found in the new samples.
Host ANP32A mediates the assembly of the influenza virus replicase.
Abstract: Host-adaptive mutations, particularly a glutamic-acid-to-lysine mutation at amino acid residue 627 (E627K) in the 627 domain of the PB2 subunit, enable avian FluPolA to overcome this restriction and efficiently replicate viral RNA in the presence of human ANP32 proteins.
Abstract: The C-terminal low-complexity acidic region of ANP32A inserts between the two juxtaposed PB2 627 domains of the asymmetric FluPolA dimer, suggesting a mechanism for how the adaptive PB2(E627K) mutation enables the replication of viral RNA in mammalian hosts.
Introduction: Such a role for the FluPol-ANP32A complex in viral genome replication is consistent with previous observations; in particular, ANP32A and the adaptive PB2 E627K mutation have
Altering Intracellular Localization of the RNA Interference Factors by Influenza A Virus Non-structural Protein 1.
Discussion: A single Glu-to-Lys substitution at position 627 of PB2 protein allows the influenza virus to infect mammalian cells more effectively and Asn at position 701 of PB2 protein is involved in the pathogenicity of the influenza virus in mice.
PA Mutations Inherited during Viral Evolution Act Cooperatively To Increase Replication of Contemporary H5N1 Influenza Virus with an Expanded Host Range.
Abstract: Clade 2.2.1 avian influenza viruses (H5N1) are unique to Egypt and generally carry the human adaptation PB2-E627K substitution during their dissemination in nature.
Abstract: These mutations were in the polymerase PA subunit and acted cooperatively with the E627K mutation in the PB2 polymerase subunit to provide higher replication in contemporary clade 2.2.1.2 viruses than in ancestral clade 2.2.1 viruses.
Introduction:
Introduction: The PB2-E627K mutation has been found in several H5N1 and H7N9 viruses that have infected humans.
Introduction: The Egyptian H5N1 clade 2.2.1 strains in poultry species generally carry the PB2-E627K mutation.
A single N342D substitution in Influenza B Virus NA protein determines viral pathogenicity in mice.
Introduction: A substitution from E to K at position 627 in the PB2 protein significantly increased the pathogenicity of avian influenza viruses (AIVs) in mice.
Enhanced Potency of a Broad H7N9-Neutralizing Antibody HNIgGA6 Through Structure-Based Design.
Introduction: H7N9 has also acquired some other mammalian-adapted genetic changes, including T271A, K526R, A588V, E627K, or D701N in the viral PB2, which facilitated viral replication and increased viral-induced disease severity in mammals.
V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.
3Introduction: Evolution modes for key mammal-adaptive mutations, including PB2-E627K, were found to differ between LPM- and patient-derived samples, indicating the dynamics of the ""genetic tuning"" of the H7N9 virus in adapting to the mammalian host."
Abstract: Notably, our findings also demonstrate the correlation between rapid host adaptation of H7N9 PB2-E627K and the fatal outcome and disease severity in humans.
Introduction: However, studies on the longitudinal dynamics of the PB2-E627K substitution of the avian-origin virus in infected patients and its influence on disease severity are lacking.
Introduction: However, the adaptive dynamics of PB2-E627K in H7N9 infected patients and the
V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.
Result: As shown in Table 1, two H9N2 viruses, A/chicken/Henan/5/1998 [CK/5(H9N2)] and A/chicken/Guangxi/9/1999 [CK/9(H9N2)], isolated in the 1990s did not acquire the PB2 E627K mutation even after being passaged six times in MDCK cells.
Result: Because our study in mice showed that PA is important for PB2 E627K acquisition during mammalian adaptation of PG/S1421(H7N9), we next investigated whether PG/S1421(H7N9), CK/5(H9N2), and their reassortants had different RNP activities in HEK293T cells.
Result: CK/5(H9N2), a representative of viruses that maintain a stable PB2 627E during replication in mammals, was selected with PG/S1421(H7N9) to form a model virus pair to investigate the viral factors that drive the emergence of the
IV mutation literature information.
PMID: 
2020
PloS one
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