Sequence analysis of P gene of human parainfluenza type 2 virus: P and cysteine-rich proteins are translated by two mRNAs that differ by two nontemplated G residues

Ohgimoto, Shinji; Bando, Hideaki; Kawano, Mitsuo; Okamoto, Kousuke; Kondo, Kunio; Tsurudome, Masato; Nishio, Machiko; Ito, Yasuhiko

doi:10.1016/0042-6822(90)90465-4

Cited by 80 publications

(49 citation statements)

References 26 publications

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“…Insertion of two residues at a specific site generates transcripts for the P protein in the case of MuV, SV5, PIV-2 and PIV-4 (Thomas et al, 1988;Elliott et al, 1990;Kondo et al, 1990;Ohgimoto et al, 1990;Paterson & Lamb, 1990;Southern et al, 1990), whereas non-edited transcripts encode the V protein. Since the porcine paramyxovirus LPMV, by analysis of its M and HN genes, is most closely related to these viruses, a similar pattern was expected.…”

Section: Discussionmentioning

confidence: 99%

“…This protein has been called I or NS2 in MuV. et al, 1990), SV5 (Thomas et aL, 1988) and PIV-2 (Ohgimoto et al, 1990). The conserved cysteine residues are boxed.…”

Section: The V Proteinmentioning

confidence: 99%

“…Based on P gene expression, the paramyxoviruses can be divided into two groups. The P gene of the first group, which includes mumps virus (MuV), simian virus 5 (SVS) and parainfluenza viruses 2 and 4 (PIV-2 and -4), contains two open reading frames (ORFs) of about equal length which overlap in the middle of the gene (Thomas et al, 1988;Elliott et al, 1990;Kondo et al, 1990;Ohgimoto et al, 1990;Paterson & Lamb, 1990;Southern et al, 1990). The N-terminal ORF encodes a protein called V, whereas the insertion of two G residues at a specific site fuses the two reading frames to express the P protein.…”

Section: Introductionmentioning

confidence: 99%

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The P gene of the procine paramyxovirus LPMV encodes three possible polypeptides P, V and C: the P protein mRNA is edited

Berg

Hjertner

Moreno‐López

et al. 1992

Journal of General Virology

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The nucleotide sequence of the P gene of the porcine paramyxovirus La-Piedad-Michoacan-Mexico virus (LPMV) was analysed. Three long open reading frames (ORFs) were found in the mRNA sense. Insertion of two G residues is necessary to obtain an ORF encoding the P protein, which gives a P protein of 404 amino acids with a calculated Mr of 42475. This form of editing was demonstrated, two non-templated G residues being added in a portion of the mRNA transcripts. The LPMV V protein, which has a conserved cysteine-rich C-terminal region, is encoded by an exact copy of the P gene. The third ORF has the capacity to encode a protein of 126 amino acids, which may resemble the C proteins found in some paramyxoviruses. The ORF starts from an AUG codon downstream of the first AUG codon of the P/V ORF.

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Section: Discussionmentioning

confidence: 99%

“…This protein has been called I or NS2 in MuV. et al, 1990), SV5 (Thomas et aL, 1988) and PIV-2 (Ohgimoto et al, 1990). The conserved cysteine residues are boxed.…”

Section: The V Proteinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The P gene of the procine paramyxovirus LPMV encodes three possible polypeptides P, V and C: the P protein mRNA is edited

Berg

Hjertner

Moreno‐López

et al. 1992

Journal of General Virology

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“…The paramyxovirus P gene also encodes other small polypeptides, V, C and C' (Thomas et al, 1988;Dethlefsen & Kolakofsky, 1983;Giorgi et al, 1983). Ohgimoto et al (1990) reported that the hPIV-2 P gene encodes the V protein and that P protein mRNA is produced by addition of two nontemplated G residues, resulting in a frameshift. The V protein is a structural protein in simian virus 5 (SV5) (Thomas et al, * Author for correspondence.…”

Section: Introductionmentioning

confidence: 99%

“…The V protein is a structural protein in simian virus 5 (SV5) (Thomas et al, * Author for correspondence. Fax +81 592 31 5008. e-mail ito @doc.medic.mie-u.ac.jp 1988), simian virus 41 (SV41) (Kawano et al, 1993), mumps virus (MuV) (Takeuchi et al, 1988) and hPIV-2 (Ohgimoto et al, 1990), but a nonstructural protein in Sendai virus (Dethlefsen & Kolakofsky, 1983;Giorgi et al, 1983) and measles virus (MV) (Bellini et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Identification of the sequences responsible for nuclear targeting of the V protein of human parainfluenza virus type 2

Watanabe¹,

Kawano²,

Tsurudome³

et al. 1996

Journal of General Virology

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In human parainfluenza virus type 2 (hPIV-2)-infected cells, anti-phosphoprotein (P)-specific monoclonal antibody (MAb) densely stained the perinuclear regions of infected cells throughout infection, indicating that the P protein was localized exclusively in the cell cytoplasm. By contrast, antigens recognized by MAbs directed against the P-V-common domain of hPIV-2 were located predominantly in the cytoplasm, but in some hPIV-2-infected cells they were also found in the nuclei, suggesting that a fraction ofhPIV-2 V protein is localized there, hPIV-2 V protein expressed from a cDNA clone was localized in the nuclei of transfected cells. By using indirect immunofluorescence analyses, we examined the intracellular localization of various sequentially deleted V proteins, to determine the nuclear localization signals (NLS) of the V protein. Two noncontiguous regions in the V protein were required for nuclear localization and retention, since deletion of these regions [region I (aa 1-46) and region II (aa ] resulted in cytoplasmic localization. Both regions resulted in nuclear localization independently. A nucleoplasmin-like NLS was identified in region II but no consensus targeting sequence could be found in region I. When NP protein was co-expressed with V protein or the Nterminal fragment (aa 1-46) of V protein, a fraction of the NP protein was translocated into cell nuclei.

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The P gene of bovine parainfluenza virus 3 expresses all three reading frames from a single mRNA editing site.

1991

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The P gene of bovine parainfluenza virus 3 (bPIV3) contains two downstream overlapping ORFs, called V and D. By comparison with the mRNA editing sites of other paramyxoviruses, two editing sites were predicted for bPIV3; site a to express the D protein, and site b to express the V protein. Examination of the bPIV3 mRNAs, however, indicates that site b is non‐functional whereas site a operates frequently. Insertions at site a give rise to both V and D protein mRNAs, because a very broad distribution of Gs is added when insertions occur. This broad distribution is very different from the editing sites of Sendai virus or SV5, where predominantly one form of edited mRNA containing either a one or two G insertion respectively is created, to access the single overlapping ORF of these viruses. A model is proposed to explain how paramyxoviruses control the range of G insertions on that fraction of the mRNAs where insertions occur. The bPIV3 P gene is unique as far as we know, in that a sizeable portion of the gene expresses all 3 reading frames as protein. bPIV3 apparently does this from a single editing site by removing the constraints which control the number of slippage rounds which take place.

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Sequence analysis of P gene of human parainfluenza type 2 virus: P and cysteine-rich proteins are translated by two mRNAs that differ by two nontemplated G residues

Cited by 80 publications

References 26 publications

The P gene of the procine paramyxovirus LPMV encodes three possible polypeptides P, V and C: the P protein mRNA is edited

The P gene of the procine paramyxovirus LPMV encodes three possible polypeptides P, V and C: the P protein mRNA is edited

Identification of the sequences responsible for nuclear targeting of the V protein of human parainfluenza virus type 2

The P gene of bovine parainfluenza virus 3 expresses all three reading frames from a single mRNA editing site.

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