H2N2V1, Main, Exploration, bibRecord, 001B81

Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses

Identifieur interne : 001B81 ( Main/Exploration ); précédent : 001B80; suivant : 001B82

Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses

Auteurs : Ping Yang ; Anju Bansal ; Chongguang Liu ; Gillian M. Air

Source :

Virology [ 0042-6822 ] ; 1997.

RBID : ISTEX:4973C23EA35B5E25A6EE9221002B8F5CD889B17F

English descriptors

Teeft :
- Amino, Amino acids, Antiserum, Cdna, Cdna clones, Cell surface, Clone, Coding information, Confluent mdck cells, Deletion, Fragment, Gene, Gene fragments, Gene segments, Hemagglutinin, Hemagglutinin activity, High levels, Immunoprecipitation, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Laver, Mdck, Mdck cells, Micromonospora viridifaciens, Mouse antiserum, Mutant, Mutant viruses, Neuraminidase, Nucleotide, Nuss, Other viruses, Palese, Peptide, Polymerase, Promega, Promoter, Rabbit antisera, Reading frame, Reassortant, Reassortant virus, Receptor, Receptor binding, Recombinant vaccinia virus, Replication, Rna, Second change, Sequencing, Sialic, Sialic acid, Sialic acids, Subgenomic, Subgenomic rnas, Terminal primers, Viral, Viridifaciens, Virion, Virology, Virology influenza viruses, Virus, Virus stock.

Abstract

Abstract: Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33HA-tern/Australia/G70c/75NA(H1N9) influenza virus in medium containing neuraminidase fromMicromonospora viridifaciensand antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.

Url:

https://api.istex.fr/ark:/67375/6H6-N3PQGW6S-0/fulltext.pdf

DOI: 10.1006/viro.1996.8421

Affiliations:

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Le document en format XML

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<term>Mutant viruses</term>
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<front><div type="abstract" xml:lang="en">Abstract: Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33HA-tern/Australia/G70c/75NA(H1N9) influenza virus in medium containing neuraminidase fromMicromonospora viridifaciensand antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.</div>
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Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses

Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri