Molecular Cloning and Sequence Analysis of Human Parainfluenza Type 2 Virus mRNA Encoding the Fusion Glycoprotein

Varsànyi, Tamas M.; Kövamees, Jan; Norrby, Erling

doi:10.1099/0022-1317-72-1-89

Cited by 8 publications

(4 citation statements)

References 35 publications

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“…Actinomycin D (5 ktg/ml) was added to the infected cell cultures 24 h before harvesting. The PDV-and CDVinfected cultures were harvested at 4 and 3 days post-infection respectively, and mRNA was extracted from the cells and purified as described by Varsanyi et al (1991).…”

Section: Methodsmentioning

confidence: 99%

Sequence analysis of the genes encoding the nucleocapsid protein and phosphoprotein (P) of phocid distemper virus, and editing of the P gene transcript

Blixenkrone-Møller¹,

Sharma

Varsànyi

et al. 1992

Journal of General Virology

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The nucleotide and deduced amino acid sequences of two genes of phocid distemper virus (PDV) were determined by cDNA cloning and sequencing. The long open reading frame of the gene encoding the nucleocapsid (N) protein is presented. As with other morbilliviruses, the phosphoprotein (P) gene of PDV was found to be located after the 5' end of the N gene and before the 3' end of the matrix protein gene. The P gene was shown to have the capacity to encode three distinct proteins, P, V and C, in analogy to other morbilliviruses. The results presented provide evidence for editing of the PDV P mRNA transcript by insertion of G residues. When the nucleotide and deduced amino acid sequences of the N, P, V and C genes were aligned with corresponding sequences of other established members of the morbillivirus genus, compelling homology was found between PDV and canine distemper virus (CDV), whereas there was markedly less similarity between PDV and measles virus or rinderpest virus. On the basis of the alignments presented, the estimated amino acid sequence similarity between the N and P genes of PDV and CDV was 84 % and 76 %, respectively. These differences at the genomic level indicate that the viruses are two separate entities.

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Section: Methodsmentioning

confidence: 99%

Sequence analysis of the genes encoding the nucleocapsid protein and phosphoprotein (P) of phocid distemper virus, and editing of the P gene transcript

Blixenkrone-Møller¹,

Sharma

Varsànyi

et al. 1992

Journal of General Virology

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“…Unlike Sendai virus and the apathogenic Newcastle disease virus strains, which possess a single arginine residue at the cleavage site of F(, occasionally in combination with another isolated arginine or lysine residue in position -4 (27), all other paramyxoviruses have multibasic cleavage sites, ranging from three to six clustered arginine or lysine residues. Thus, the F precursor proteins of hPIV2 and hPIV3 have the sequences R-Q-K-R and R-T-K-R, respectively, at the cleavage site (6,11,22,25,28). The consensus sequence R-X-K/R-R is also present in glycoproteins of other enveloped viruses, e.g., retroviruses and cytomegalovirus, as well as in a great number of cellular proproteins, such as the precursors of anthrax toxin, Marburg, Germany.…”

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confidence: 99%

Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2

Ortmann

Ohuchi

Angliker

et al. 1994

J Virol

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The fusion (F) protein of human parainfluenza virus type 3 contains the tribasic cleavage site R-T-K-R, which was altered by site-directed mutagenesis. Wild-type F protein and various mutants were expressed by recombinant vaccinia viruses. The endogenous endoprotease present in CV-1 cells cleaves F variants containing the furin recognition motif R-X-K/R-R but not variants containing the dibasic site K-R or a single R at the cleavage site. A similar cleavage pattern was obtained when the subtilisin-like endoproteases Kex2 and furin were coexpressed with the wild type and mutants of the F protein. Peptidylchloromethylketone inhibitors mimicking basic cleavage sites prevent cleavage of the precursor Fo by the endogenous protease only when the furin-specific motif is present in the peptidyl portion. The data support the concept that furin is a cellular protease responsible for the activation of the F protein of human parainfluenza virus type 3.

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“…Indirect immunofluorescence indicated that about 30% of all cells expressed the viral surface antigen H protein at this time. The cells were harvested 4 days p.i., and mRNA was extracted and purified as described (Varsanyi et al, 1991).…”

Section: Methodsmentioning

confidence: 99%

The Nucleotide Sequence and Deduced Amino Acid Composition of the Haemagglutinin and Fusion Proteins of the Morbillivirus Phocid Distemper Virus

Kövamees

Blixenkrone-Møller²,

Sharma³

et al. 1991

Journal of General Virology

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The amino acid composition of the two surface proteins of the recently isolated morbillivirus phocid distemper virus (PDV) were deduced from the nucleotide sequence. The fusion (F) protein of PDV exhibited characteristics similar to those of other morbillivirus F proteins. The overall amino acid similarity with its closest homologue, canine distemper virus (CDV), was 72%. From the context of the starting codons and the requirement for a hydrophobic signal peptide, it is likely that translation of the PDV F mRNA starts at the third AUG, corresponding to codon 95 in the long open reading frame of the PDV F gene. After removal of the signal peptide, F0 starts at amino acid 105. From this position the F protein of PDV and CDV exhibit 84% amino acid similarity. The PDV haemagglutinin (H) protein showed 74% amino acid similarity with CDV H protein and highly conserved features responsible for the tertiary structure. Despite these similarities, the two H proteins show marked antigenic differences when probed with monoclonal antibodies. Earlier studies have indicated that rinderpest virus (RPV) is the prototype virus of the morbillivirus genus, from which first CDV/PDV and later measles virus (MV) evolved. From the close relationship shown in this study, it is likely that the divergence of CDV and PDV occurred after MV evolved from RPV.

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Molecular Cloning and Sequence Analysis of Human Parainfluenza Type 2 Virus mRNA Encoding the Fusion Glycoprotein

Cited by 8 publications

References 35 publications

Sequence analysis of the genes encoding the nucleocapsid protein and phosphoprotein (P) of phocid distemper virus, and editing of the P gene transcript

Sequence analysis of the genes encoding the nucleocapsid protein and phosphoprotein (P) of phocid distemper virus, and editing of the P gene transcript

Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2

The Nucleotide Sequence and Deduced Amino Acid Composition of the Haemagglutinin and Fusion Proteins of the Morbillivirus Phocid Distemper Virus

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