Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity
Identifieur interne : 000393 ( Istex/Curation ); précédent : 000392; suivant : 000394Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity
Auteurs : G. M. Air [États-Unis] ; L. R. Ritchie [États-Unis] ; W. G. Laver [Australie] ; P. M. Colman [Australie]Source :
- Virology [ 0042-6822 ] ; 1985.
English descriptors
- Teeft :
- Amino, Amino acid, Amino acid sequence, Amino acids, Antigenic sites, Buffer gradient, Cdna, Cdna copy, Coding information, Dideoxy method, Ecori sites, Hemagglutinating neuraminidase, Hemagglutinin, Influenza, Influenza virus, Influenza virus neuraminidase, Laver, Neuraminidase, Neuraminidase gene, Nucleic acids, Nucleotide, Nucleotide sequence, Nucleotide sequence coding, Other influenza, Peptide, Plasmid puc9, Primer, Protein sequence, Sequence analysis, Sequencing, Sialic acid binding site, Subtype sequences, Synthetic oligonucleotides, Tryptic peptides, Universal primer, Virology, Virus neuraminidase.
Abstract
Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.
Url:
DOI: 10.1016/0042-6822(85)90206-5
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<term>Buffer gradient</term>
<term>Cdna</term>
<term>Cdna copy</term>
<term>Coding information</term>
<term>Dideoxy method</term>
<term>Ecori sites</term>
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<term>Nucleic acids</term>
<term>Nucleotide</term>
<term>Nucleotide sequence</term>
<term>Nucleotide sequence coding</term>
<term>Other influenza</term>
<term>Peptide</term>
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<term>Primer</term>
<term>Protein sequence</term>
<term>Sequence analysis</term>
<term>Sequencing</term>
<term>Sialic acid binding site</term>
<term>Subtype sequences</term>
<term>Synthetic oligonucleotides</term>
<term>Tryptic peptides</term>
<term>Universal primer</term>
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<front><div type="abstract" xml:lang="en">Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.</div>
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