Sequence of the hemagglutinin gene from influenza virus A/Seal/Mass/1 /80
Identifieur interne : 002580 ( Main/Exploration ); précédent : 002579; suivant : 002581Sequence of the hemagglutinin gene from influenza virus A/Seal/Mass/1 /80
Auteurs : Clayton W. Naeve [États-Unis] ; Robert G. Webster [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1983.
English descriptors
- Teeft :
- Academic press, Acid, Acid sequence, Additional prolines, Amino, Amino acid, Amino acid sequence, Amino acid sequences, Amino acids, Antigenic, Antigenic drift, Antigenic studies, Antigenic variation, Avian, Avian influenza virus, Avian influenza viruses, Avian strains, Avirulent, Avirulent strains, Base composition, Bosch, Brownlee, Cdna, Cleavage, Cleavage activation, Complete nucleotide, Differences homology, Glycosylation, Glycosylation site, Graphic matrix analysis, Hemagglutinin, Hemagglutinin gene, Hemagglutinins, Hinshaw, Hong kong, Host cell receptors, Host cells, Host range, Human influenza virus, Important residues, Influenza, Influenza hemagglutinin, Influenza virus, Influenza virus hemagglutinin, Influenza viruses, Klenk, Klenow fragment, Laver, Mammalian origin, Matrix analysis, Methods enzymol, Monoclonal antibodies, Nucleic acid, Nucleic acids, Nucleotide, Nucleotide differences, Nucleotide sequence, Peptide, Peptide region, Personal communication, Polynucleotide kinase, Positive clones, Potential glycosylation sites, Primary structure, Primer, Proline, Proteolytic cleavage, Restriction fragments, Seal influenza virus hemagglutinin, Seal sequence, Seal virus, Second line, Secondary structure, Sequence information, Sequencing, Serotype, Signal peptide, Structural differences, Synthetic primer, Tertiary structure, Virology, Virus, Webster, Wider variety.
Abstract
Abstract: A double-strand DNA copy of the influenza virus A/Seal/Mass/1/80 (H7N7) [seal] hemagglutinin (HA) gene was cloned into the plasmid pAT153/PvuII/8 and sequenced to deduce the primary amino acid sequence. The gene is 1731 nucleotides long and codes for a protein of 560 amino acids with a nonglycosylated molecular weight of 62098 Da. The deduced amino acid sequence displays similarities to all other sequenced hemagglutinins by retaining six of seven potential glycosylation sites, showing conversation in the number and position of cysteine residues, conservation in the fusion and anchor peptides, and conservation in the putative receptor site of the molecule. However, three features of the primary amino acid sequence could be distinguished from the H7 amino acid sequence of A/fowl plague/Rostock/34 (FPV), another avian H7 influenza virus which does not produce disease in mammals. First, the seal HA sequence has three fewer amino acids in the connecting peptide region of the HA than FPV. This lack of multiple basic amino acids in the connecting peptide is similar to that found in avirulent H7 avian strains and to mammalian serotypes Hl, H2, and H3. Second, the seal HA has gained four additional proline residues, all in HA1, as compared to FPV. These residues may alter the tertiary structure of the HA and ultimately contribute to the biological features of this virus. Third, the seal HA has lost a potential carbohydrate attachment site at residue 149 which lies at the tip of the HA structure. The loss of this carbohydrate could alter the seal HAs interaction with host cell receptors.
Url:
DOI: 10.1016/0042-6822(83)90169-1
Affiliations:
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The gene is 1731 nucleotides long and codes for a protein of 560 amino acids with a nonglycosylated molecular weight of 62098 Da. The deduced amino acid sequence displays similarities to all other sequenced hemagglutinins by retaining six of seven potential glycosylation sites, showing conversation in the number and position of cysteine residues, conservation in the fusion and anchor peptides, and conservation in the putative receptor site of the molecule. However, three features of the primary amino acid sequence could be distinguished from the H7 amino acid sequence of A/fowl plague/Rostock/34 (FPV), another avian H7 influenza virus which does not produce disease in mammals. First, the seal HA sequence has three fewer amino acids in the connecting peptide region of the HA than FPV. This lack of multiple basic amino acids in the connecting peptide is similar to that found in avirulent H7 avian strains and to mammalian serotypes Hl, H2, and H3. Second, the seal HA has gained four additional proline residues, all in HA1, as compared to FPV. These residues may alter the tertiary structure of the HA and ultimately contribute to the biological features of this virus. Third, the seal HA has lost a potential carbohydrate attachment site at residue 149 which lies at the tip of the HA structure. The loss of this carbohydrate could alter the seal HAs interaction with host cell receptors.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Naeve, Clayton W" sort="Naeve, Clayton W" uniqKey="Naeve C" first="Clayton W." last="Naeve">Clayton W. Naeve</name></noRegion><name sortKey="Webster, Robert G" sort="Webster, Robert G" uniqKey="Webster R" first="Robert G." last="Webster">Robert G. Webster</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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