Fusion glycoprotein of human parainfluenza virus type 3: Nucleotide sequence of the gene, direct identification of the cleavage-activation site, and comparison with other paramyxoviruses
Identifieur interne : 002375 ( Main/Exploration ); précédent : 002374; suivant : 002376Fusion glycoprotein of human parainfluenza virus type 3: Nucleotide sequence of the gene, direct identification of the cleavage-activation site, and comparison with other paramyxoviruses
Auteurs : Melanie K. Spriggs [États-Unis] ; Robert A. Olmsted [États-Unis] ; Sundararajan Venkatesan [États-Unis] ; John E. Coligan [États-Unis] ; Peter L. Collins [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1986.
English descriptors
- Teeft :
- Academic press, Acid sequence, Acid sequencing, Amino, Amino acid, Amino acid sequences, Amino acids, Cdna, Cdna clones, Cdna sequence, Cellular protease, Chemical method, Choppin, Cleavage, Cleavage site, Clone, Cysteine, Cysteine residues, Dideoxynucleotide, Dideoxynucleotide sequencing, Fusion protein, Glycoprotein, Homology, Human parainfluenza virus type, Influenza, Influenza virus, Influenza viruses, Membrane anchor, Mrna, Nucleotide, Nucleotide sequence, Parainfluenza, Paramyxovirus, Paramyxovirus glycoproteins, Peptide, Primer, Protein, Proteolytic, Proteolytic cleavage, Respiratory syncytial virus, Sendai, Sendai virus, Sequencing, Signal peptide, Spriggs, Subunit, Synthetic oligonucleotide primers, Terminus, Vesicular stomatitis virus, Viral, Virion, Virology, Virus, Vrna.
Abstract
Abstract: The complete sequences of the fusion (F) mRNA and protein of human parainfluenza virus type 3 (PF3) were determined from overlapping cDNA clones. To confirm the cDNA sequence, the complete sequence of the F gene was determined independently by dideoxynucleotide sequencing of genomic RNA using synthetic oligonucleotide primers. The mRNA contains 1845 nucleotides, exclusive of poly (A), has an unusually long (193-nucleotide) 5′ nontranslated region, and encodes an F0 protein of 539 amino acids. The site within F0 of the proteolytic cleavage that activates fusion activity was established by direct amino acid sequencing of the NH2 terminus of the F1 subunit. The PF3 F0 protein shares major structural features with the previously sequenced F0 proteins of Sendai virus (murine parainfluenza type 1) and simian virus 5 (SV5, canine parainfluenza type 2), including: similarity in overall length; similarity in location of the site of the activating proteolytic cleavage; the presence of an NH2-terminal signal peptide and COOH-proximal membrane anchor; strong conservation of the sequence at the NH2 terminus of the F1 subunit; and nearly exact conservation in the number and positions of cysteine residues. Alignment of the F0 protein sequences of PF3 with those of Sendai, SV5, and respiratory syncytial virus (RSV) using a matrix that stores both amino acid matches and mismatches provided highly significant statistical evidence that all four proteins are related. The order of decreasing relatedness to PF3 was found to be: Sendai virus, SV5, and RSV.
Url:
DOI: 10.1016/0042-6822(86)90388-0
Affiliations:
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To confirm the cDNA sequence, the complete sequence of the F gene was determined independently by dideoxynucleotide sequencing of genomic RNA using synthetic oligonucleotide primers. The mRNA contains 1845 nucleotides, exclusive of poly (A), has an unusually long (193-nucleotide) 5′ nontranslated region, and encodes an F0 protein of 539 amino acids. The site within F0 of the proteolytic cleavage that activates fusion activity was established by direct amino acid sequencing of the NH2 terminus of the F1 subunit. The PF3 F0 protein shares major structural features with the previously sequenced F0 proteins of Sendai virus (murine parainfluenza type 1) and simian virus 5 (SV5, canine parainfluenza type 2), including: similarity in overall length; similarity in location of the site of the activating proteolytic cleavage; the presence of an NH2-terminal signal peptide and COOH-proximal membrane anchor; strong conservation of the sequence at the NH2 terminus of the F1 subunit; and nearly exact conservation in the number and positions of cysteine residues. Alignment of the F0 protein sequences of PF3 with those of Sendai, SV5, and respiratory syncytial virus (RSV) using a matrix that stores both amino acid matches and mismatches provided highly significant statistical evidence that all four proteins are related. The order of decreasing relatedness to PF3 was found to be: Sendai virus, SV5, and RSV.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Spriggs, Melanie K" sort="Spriggs, Melanie K" uniqKey="Spriggs M" first="Melanie K." last="Spriggs">Melanie K. Spriggs</name></noRegion><name sortKey="Coligan, John E" sort="Coligan, John E" uniqKey="Coligan J" first="John E." last="Coligan">John E. Coligan</name><name sortKey="Collins, Peter L" sort="Collins, Peter L" uniqKey="Collins P" first="Peter L." last="Collins">Peter L. Collins</name><name sortKey="Olmsted, Robert A" sort="Olmsted, Robert A" uniqKey="Olmsted R" first="Robert A." last="Olmsted">Robert A. Olmsted</name><name sortKey="Venkatesan, Sundararajan" sort="Venkatesan, Sundararajan" uniqKey="Venkatesan S" first="Sundararajan" last="Venkatesan">Sundararajan Venkatesan</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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