M protein correlates with the receptor-binding specificity of haemagglutinin protein of reassortant influenza A (H1N1) virus.

Tong, N; Nobusawa, Eri; Morishita, Masaki; Nakajima, Setsuko; Nakajima, Kazuki

doi:10.1099/0022-1317-79-10-2425

Cited by 16 publications

(15 citation statements)

References 29 publications

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“…The M1 protein is a strong candidate for this novel role, because it differs in both HKMA20 and HKMA20C relative to HKMA12 and has been implicated in the modulation of HA function. Strains of human influenza H1N1 viruses with identical HA molecules differ in their ability to agglutinate chick erythrocytes because of the nature of their M1 proteins (23). Interestingly, fixation of the M1-167 mutation in the human lineage in 1972 coincided with a change in receptor specificity (24) that did not correlate with changes in HA sequence, again suggesting the involvement of another protein in HA function.…”

Section: Ma Variants Possess Mutations In Specific Functionalmentioning

confidence: 82%

Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: Identification of functional themes

Brown

Liu

Kit

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

174

152

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The genetic basis for virulence in influenza virus is largely unknown. To explore the mutational basis for increased virulence in the lung, the H3N2 prototype clinical isolate, A͞HK͞1͞68, was adapted to the mouse. Genomic sequencing provided the first demonstration, to our knowledge, that a group of 11 mutations can convert an avirulent virus to a virulent variant that can kill at a minimal dose. Thirteen of the 14 amino acid substitutions (93%) detected among clonal isolates were likely instrumental in adaptation because of their positive selection, location in functional regions, and͞or independent occurrence in other virulent influenza viruses. Mutations in virulent variants repeatedly involved nuclear localization signals and sites of protein and RNA interaction, implicating them as novel modulators of virulence. Mouse-adapted variants with the same hemagglutinin mutations possessed different pH optima of fusion, indicating that fusion activity of hemagglutinin can be modulated by other viral genes. Experimental adaptation resulted in the selection of three mutations that were in common with the virulent human H5N1 isolate A͞HK͞ 156͞97 and that may be instrumental in its extreme virulence. Analysis of viral adaptation by serial passage appears to provide the identification of biologically relevant mutations.

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Section: Ma Variants Possess Mutations In Specific Functionalmentioning

confidence: 82%

Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: Identification of functional themes

Brown

Liu

Kit

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

174

152

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“…Parent A/Memphis/1/71 strain did not show binding to the sialylglycolipids except IV 6 (Neu5Ac)nLc 4 B30 on virus overlay assay. The discrepancy in the binding pattern between WT and A/Memphis/1/71 may be due to matrix protein 1 (M1) of A/WSN/33, which affects binding affinity by interaction with HA at the inner membrane of the virus envelope [13]. N137Y and S193N exhibited the same binding pattern as that of A/Memphis/ 1/71 strain (Figs.…”

Section: Resultsmentioning

confidence: 99%

Identification of amino acid residues of influenza A virus H3 HA contributing to the recognition of molecular species of sialic acid

et al. 2009

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a b s t r a c tTo identify a determinant of human H3 hemagglutinin (HA) amino acid residues linked to the recognition of molecular species of sialic acid, we generated six mutant viruses possessing either the wild-type HA gene from A/Memphis/1/71 (H3N2) or a genetically single-mutated HA gene at position 137, 144, 155, 158 or 193 from a genetic backbone of A/WSN/33 (H1N1) by reverse genetics. We evaluated the binding ability with four types of synthetic sialylglycolipids. The results indicate that the amino acid substitutions Thr155 to Tyr and Glu158 to Gly in H3 HA facilitate virus binding to N-glycolylneuraminic acid.

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“…In order that such adsorption provokes a conformational change in the hemagglutinin, which is a trimer, it must be triggered off by the action of host's proteases in a hemagglutinin site called 'cleavage site' (Tong et al 1998). The endosome's pH formed after adsorption and virus penetration is decisive for the fusion of the viral envelope with the cell membrane culminating in the success of the infection, when it is possible to observe the conformational changes of hemagglutinin that allow such fusion (Wharton et al 1995).…”

Section: Introductionmentioning

confidence: 99%

Seroprevalence of H3n2 Influenza a Virus in Pigs From Paraná (South Brazil): Interference of the Animal Management and Climatic Conditions

Caron

Joineau²,

Santín³

et al. 2010

VR&R

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M protein correlates with the receptor-binding specificity of haemagglutinin protein of reassortant influenza A (H1N1) virus.

Cited by 16 publications

References 29 publications

Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: Identification of functional themes

Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: Identification of functional themes

Identification of amino acid residues of influenza A virus H3 HA contributing to the recognition of molecular species of sialic acid

Seroprevalence of H3n2 Influenza a Virus in Pigs From Paraná (South Brazil): Interference of the Animal Management and Climatic Conditions

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