Molecular relationships between human parainfluenza virus type 2, and simian viruses 41 and 5: determination of nucleoprotein gene sequences of simian viruses 41 and 5

Tsurudome, Masato; Oki, Naohiro; Higuchi, Yasumitsu; Miyahara, K.; Yoshimoto, Momoko; Mutsuga, Naomi; Kitada, Shuichi; Ogawa, Masahiro; Miyahara, Yoshihiro; Okamoto, Katsushi; Kawano, Mitsuo; Komada, Hiroshi; Matsumura, Haruo; Kusagawa, Shigeru; Nishio, Machiko; Ito, Yasuhiko

doi:10.1099/0022-1317-72-9-2289

Cited by 7 publications

(4 citation statements)

References 21 publications

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“…hPIV2, SV41, and PIV5 are all rubulaviruses, and their proteins have highly homology. The NP proteins of hPIV2 and the more distantly related PIV5 are 57.0% identical at the amino acid level, the P proteins are 39.8% identical, and the L proteins are 63.9% identical (19,43,58). In order to assess which combinations of the NP, P, and L proteins were able to cooperate in the minigenome system of hPIV2, all possible combinations of the NP, P, and L proteins derived from hPIV2 and PIV5 were tested (Fig.…”

Section: Resultsmentioning

confidence: 99%

Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness

Nishio

Ohtsuka

Tsurudome

et al. 2008

J Virol

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The human parainfluenza virus type 2 (hPIV2) V protein plays important roles in inhibiting the host interferon response and promoting virus growth, but its role in hPIV2 replication and transcription is not clear. A green fluorescent protein (GFP)-expressing a negative-sense minigenomic construct of hPIV2 has been established by standard technology, with helper plasmids expressing the nucleocapsid protein (NP), phosphoprotein (P), and large RNA polymerase (L) protein, to examine the role of V protein. We found that the simultaneous expression of wild-type V protein in the minigenome system inhibited GFP expression, at least in part, by inhibiting minigenome replication. In contrast, expression of C terminally truncated or mutant hPIV2 V proteins had no effect. Moreover, the V protein of simian virus 41, the rubulavirus most closely related virus to hPIV2, also inhibited GFP expression, whereas that of PIV5, a more distantly related rubulavirus, did not. Using these other rubulavirus V proteins, as well as various mutant hPIV2 V proteins, we found that the ability of V protein to inhibit GFP expression correlated with its ability to bind to L protein via its C-terminal V protein-specific region, but there was no correlation with NP binding. A possible role for this inhibition of genome replication in promoting viral fitness is discussed.Human parainfluenza virus type 2 (hPIV2) is a member of the Rubulavirus genus of the family Paramyxoviridae. This family includes many well-known human and animal pathogens, such as Sendai virus (SeV), hPIV types 1 to 4, simian virus 41 (SV41), parainfluenza virus type 5 (PIV5; formerly known as SV5), mumps virus, Newcastle disease virus, measles virus (MeV), and respiratory syncytial virus, as well as important emerging viruses such as Hendra and Nipah viruses. The negative-stranded RNA genome of hPIV2 is 15,654 nucleotides long and encodes seven viral proteins from six genes (30). The nucleocapsid protein (NP), phosphoprotein (P), and large RNA polymerase (L) protein are important for transcription and replication of the viral RNA genome. All viruses of the Paramyxoviridae (with the notable exception of hPIV1) contain an mRNA-editing site at which G residues are inserted into the P gene mRNA in a programmed manner during its synthesis. In respiroviruses and morbilliviruses, the P mRNA is a faithful copy of the genome RNA, and the V mRNA results from the insertion of one additional pseudotemplated G nucleotide. In only rubulaviruses, it is the V mRNA that is a faithful transcript of the V/P gene, whereas the P mRNA is synthesized through a cotranscriptional insertion of two pseudotemplated G residues. Thus, the N-terminal 164 amino acids (aa) of the V and P proteins are common, while their C termini are unique (43). Since insertion of the G residues in hPIV2 occurs ca. 50% of the time, roughly equal amounts of V and P mRNAs are produced. The C termini of the V proteins contain seven invariant cysteines that bind two atoms of zinc and is ca. 50% identical in sequence among all par...

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Section: Resultsmentioning

confidence: 99%

Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness

Nishio

Ohtsuka

Tsurudome

et al. 2008

J Virol

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“…It has been reported that elongation of the cytoplasmic tail of the influenza virus HA protein by as little as 1 amino acid reduced fusion activity significantly, whereas the addition of 5 amino acids abolished fusion activity completely (Ohuchi et al, 1998). On the other hand, the length of the cytoplasmic tail of the SER F protein is comparable to that of SV-41 F, which is the longest among the paramyxovirus F proteins (Tsurudome et al, 1991). Since the SV-41 F protein is able to induce cell fusion, the specific amino acids sequence of the SER F C-tail rather than the length appears to be a more important factor in the regulation of membrane fusion activity.…”

Section: Fig 10mentioning

confidence: 98%

Regulation of Fusion Activity by the Cytoplasmic Domain of a Paramyxovirus F Protein

Tong

Vincent

et al. 2002

Virology

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SER virus is a member of the family Paramyxoviridae, genus Rubulavirus, which has been isolated from pigs. It is very closely related to SV5 virus serologically, in protein profile, and in nucleotide sequence. However, unlike SV5, SER induces minimal syncytium formation in infected CV-1 or BHK cells. Fluorescence transfer experiments between labeled erythrocytes and infected MDBK cells revealed that SER also induces hemifusion and pore formation with reduced efficiency. The virion polypeptide profiles of SER and SV5 are very similar, except that the SER F1 subunit shows an apparent molecular weight that is about 2 kDa higher than that of SV5. Comparison of the deduced amino acid sequences revealed the SER F (551 aa) to be longer than SV5 F (529 aa) by 22 residues in the cytoplasmic tail (CT) domain. The HN and M gene sequences of the viruses were found to be very similar. The SER F showed minimal fusion activity when coexpressed with either SV5 or SER HN. In contrast, SV5 F was highly fusogenic when coexpressed with either HN protein, indicating that the restricted fusion capacity of SER virus is a property of its F protein. Truncation in the CT of SER F by 22 residues completely rescued its ability to cause syncytium formation, whereas other truncations rescued syncytium formation partially. These results demonstrate that an elongated CT of a paramyxovirus F protein suppresses its membrane fusion activity.

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“…A comparison of the Mapuera virus N protein sequence with that of the other paramyxoviruses revealed 55 % identity with mumps virus (Elango et al, 1989), 54 % with SV5 (Tsurudome et al, 1991), 51% with SV41 (Tsurudome et al, 1991) and HPIV2 (Yuasa et al, 1990), 50% with HPIV type 4a/b and only 35% with NDV (Ishida et al, 1986). Lower levels of identity were found when Mapuera virus N protein was compared to the measles virus N protein (28 %) and Sendai virus N protein (21%).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Mapuera virus: structure, proteins and nucleotide sequence of the gene encoding the nucleocapsid protein

Henderson¹,

Laird²,

Dermott³

et al. 1995

Journal of General Virology

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The molecular biology of Mapuera virus was studied at both the protein and nucleic acid levels. Seven virusencoded proteins were detected in infected Vero cells. The sizes and characteristics of each of the proteins determined from various radiolabelling experiments allowed preliminary identification of the proteins as the large (L; 190 kDa), haemagglutinin neuraminidase (HN; 74 kDa), nucleocapsid (N; 66 kDa), fusion (Fo; 63 kDa), phosphoprotein (P; 49 kDa), matrix (M; 43 kDa) and non-structural (V; 35kDa) proteins. Western blot analysis showed that the HN, N and P proteins were major antigens recognized in the mouse. A cDNA library of total virus-infected cellular mRNA was created and screening of the library resulted in the detection of cDNA sequences representing the N mRNA transcript of Mapuera virus. The N mRNA sequence determined from the clones was 1731 nt in length and contained an ORF that encoded 537 amino acids, the complete 3' untranslated region and part of the 5' non-coding region. The calculated M r of the N protein was 59 kDa, which is close to the 66 kDa protein observed by SDS-PAGE.

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Molecular relationships between human parainfluenza virus type 2, and simian viruses 41 and 5: determination of nucleoprotein gene sequences of simian viruses 41 and 5

Cited by 7 publications

References 21 publications

Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness

Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness

Regulation of Fusion Activity by the Cytoplasmic Domain of a Paramyxovirus F Protein

Characterization of Mapuera virus: structure, proteins and nucleotide sequence of the gene encoding the nucleocapsid protein

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