Variation in the membrane-insertion and "stalk" sequences in eight subtypes of influenza type A virus neuraminidase

Blok, J.; Air, Gillian M.

doi:10.1021/bi00260a015

Cited by 65 publications

(36 citation statements)

References 47 publications

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“…RT-PCR with primer sets that amplified the 5' end of the neuraminidase gene segments further showed that these viruses were of the N1 genotype. Nucleotide sequence analysis and comparison with published neuraminidase sequences 20 confirmed this finding genetically ( figure 2).…”

supporting

confidence: 69%

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

et al. 1998

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supporting

confidence: 69%

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

et al. 1998

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“…When sequences of human N2 NAs from 1957 to 1998 are compared, regions of high variability can be seen. As previously noted, the stalk region is highly variable but has not been associated with the binding of neutralizing antibodies (2,5,9). The variable regions in the NA "head" domain are amino acids 140 to 155, 328 to 370, and to a lesser extent 381 to 403.…”

Section: Discussionmentioning

confidence: 82%

Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)

Gulati

Hwang

Venkatramani

et al. 2002

J Virol

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100

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“…27) and 51 (NA; ref. 28) amino acids, respectively. If they are predominantly ␣-helical, this would correspond to stem lengths of 1.5 and 7.6 nm, respectively, in general accord with our measurements.…”

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.

464

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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Variation in the membrane-insertion and "stalk" sequences in eight subtypes of influenza type A virus neuraminidase

Cited by 65 publications

References 47 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

Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)

Influenza virus pleiomorphy characterized by cryoelectron tomography

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