Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses

Nobusawa, Eri; Aoyama, Toru; Kato, Hideshige; Suzuki, Yasuo; Tateno, Yoshio; Nakajima, Kazuki

doi:10.1016/0042-6822(91)90588-3

Cited by 456 publications

(353 citation statements)

References 32 publications

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“…When the aminoacids expected to be involved in the assembly of the receptor binding site on the haemagglutinin 15,16 were examined, no differences were observed between the human and avian H5 The GCG Wisconsin package was used to FETCH sequences from GenBank. Multiple sequence files were generated and analysed by DNAPARS in the PHYLIP package.…”

mentioning

confidence: 99%

Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus

et al. 1998

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mentioning

confidence: 99%

Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus

et al. 1998

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“…Between the ectodomain sequences and the predicted transmembrane regions are linkers of 10 (HA; ref. 27) and 51 (NA; ref. 28) amino acids, respectively.…”

Section: Influenza Virusmentioning

confidence: 99%

“…28) and 10 residues (HA; ref. 27). The existence of direct interactions of the glycoproteins with the matrix layer is further supported by the correlation of gaps in the matrix layer with membrane regions in which the glycoproteins are either absent or less abundant than elsewhere (Fig.…”

Section: Influenza Virusmentioning

confidence: 99%

Influenza virus pleiomorphy characterized by cryoelectron tomography

Harris

Cardone

Winkler

et al. 2006

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

462

542

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Influenza virus remains a global health threat, with millions of infections annually and the impending threat that a strain of avian influenza may develop into a human pandemic. Despite its importance as a pathogen, little is known about the virus structure, in part because of its intrinsic structural variability (pleiomorphy): the primary distinction is between spherical and elongated particles, but both vary in size. Pleiomorphy has thwarted structural analysis by image reconstruction of electron micrographs based on averaging many identical particles. In this study, we used cryoelectron tomography to visualize the 3D structures of 110 individual virions of the X-31 (H3N2) strain of influenza A. The tomograms distinguish two kinds of glycoprotein spikes [hemagglutinin (HA) and neuraminidase (NA)] in the viral envelope, resolve the matrix protein layer lining the envelope, and depict internal configurations of ribonucleoprotein (RNP) complexes. They also reveal the stems that link the glycoprotein ectodomains to the membrane and interactions among the glycoproteins, the matrix, and the RNPs that presumably control the budding of nascent virions from host cells. Five classes of virions, four spherical and one elongated, are distinguished by features of their matrix layer and RNP organization. Some virions have substantial gaps in their matrix layer (''molecular fontanels''), and others appear to lack a matrix layer entirely, suggesting the existence of an alternative budding pathway in which matrix protein is minimally involved.envelope glycoproteins ͉ matrix protein ͉ ribonucleoprotein particles ͉ virus assembly ͉ virus structure

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“…Comprehensive comparison of HA cleavage sites and their adjacent regions have revealed that H5 HPAIVs carry, at position 346 (corresponding position 323 according to H3 numbering; Ha et al, 2001;Nobusawa et al, 1991), either serine or threonine, with the exception of few strains. In contrast, almost all LPAIVs strains possess valine at this position.…”

Section: Generation Of Recombinant Virusesmentioning

confidence: 99%

Amino acids adjacent to the haemagglutinin cleavage site are relevant for virulence of avian influenza viruses of subtype H5

Gohrbandt

Veits

Hundt

et al. 2010

Journal of General Virology

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The prime virulence determinant of highly pathogenic avian influenza viruses (HPAIVs) is the polybasic haemagglutinin (HA) cleavage site. However, engineering of a polybasic cleavage site into an avian influenza virus of low pathogenicity does not result in transformation into an HPAIV, indicating the importance of other adaptations. Here, the influence of amino acids adjacent to the HA cleavage site on virulence was studied. Most HPAIVs of subtype H5 carry serine or threonine at position 346 (corresponding to position 323 according to H3 numbering), whereas almost all low-pathogenic H5 viruses have valine. Moreover, all H5 low-pathogenic strains carry threonine at position 351 (corresponding to position 328 according to H3 numbering), suggesting that acquisition of a polybasic cleavage site involves several steps. This study generated a virus mutant derived from HPAIV A/Swan/Germany/R65/06 H5N1 (R65) with a monobasic cleavage site, R65 mono -S-ER, and the following additional mutants: R65 mono -V-ER with serine changed to valine at position 346, and R65 mono -S-ETR and R65 mono -V-ETR with threonine inserted at position 351. Moreover, in the R65 HA, serine was replaced with valine at position 346 (R65-V). Infection of chickens with R65 mono -S-ETR or R65 mono -S-ER led to slight transient respiratory symptoms, whereas R65-infected animals died within 2 days. However, chickens infected with R65-V survived longer than R65-infected animals, indicating that serine 346 in R65 HA contributes to virulence. These data suggest that evolution of H5 HPAIVs from low-pathogenic precursors, besides acquisition of a polybasic cleavage site, involves adaptation of neighbouring regions.

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Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses

Cited by 456 publications

References 32 publications

Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus

Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus

Influenza virus pleiomorphy characterized by cryoelectron tomography

Amino acids adjacent to the haemagglutinin cleavage site are relevant for virulence of avian influenza viruses of subtype H5

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