The Mumps Virus SH Protein Is a Membrane Protein and Not Essential for Virus Growth

Takeuchi, Kaoru; Tanabayashi, Kiyoshi; Hishiyama, Michiko; Yamada, Akio

doi:10.1006/viro.1996.0583

Cited by 86 publications

(55 citation statements)

References 3 publications

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“…Staining against protein disulfide isomerase (PDI) demonstrated that the SH protein was localized in the ER (Fig. 3b), as reported previously by Takeuchi et al (1996). When pHA-SH wt and pMyc-A1Up were co-expressed, SH was partially redistributed to co-localize with A1Up and the 20S proteasome in the aforementioned punctate structures (Fig.…”

Section: Subcellular Localization Of A1up and Shsupporting

confidence: 80%

“…Recently a new genotype, M, was described (Santos et al, 2008). The SH (small hydrophobic) protein of MuV is expressed in MuV-infected cells but is not a constituent part of the virion (Takeuchi et al, 1996). SH is apparently non-essential for viral replication in cell culture, since the growth rate of cell culture-adapted strain Enders, which does not express the SH protein, is not restricted compared with wild-type MuV strains (Afzal et al, 1990;Takeuchi et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

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Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)

Woznik

Rödner²,

Lemon

et al. 2010

Journal of General Virology

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The small hydrophobic (SH) protein of mumps virus has been reported to interfere with innate immunity by inhibiting tumour necrosis factor alpha-mediated apoptosis. In a yeast two-hybrid screen we have identified the ataxin-1 ubiquitin-like interacting protein (A1Up) as a cellular target of the SH protein. A1Up contains an amino-terminal ubiquitin-like (UbL) domain, a carboxyterminal ubiquitin-associated (UbA) domain and two stress-inducible heat shock chaperoninbinding (Sti1) motifs. This places it within the ubiquitin-like protein family that is involved in proteasome-mediated activities. Co-immunoprecipitation confirmed the binding of SH and A1Up and demonstrates that a truncated protein fragment corresponding to aa 136-270 of A1Up, which represents the first Sti1-like repeat and an adjacent hydrophobic region, was sufficient for interaction, whereas neither the UbL nor the UbA domains were required for interaction. The ectopic expression of A1Up leads to a redistribution of SH to punctate structures that co-localize with the 20S proteasome in transfected or infected mammalian cells.

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Section: Subcellular Localization Of A1up and Shsupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)

Woznik

Rödner²,

Lemon

et al. 2010

Journal of General Virology

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“…The SH gene of MuV is 316 nucleotides long and encodes a protein of 57 amino acids that is detected in MuV-infected cells (13). The SH gene is the most heterogeneous in comparison with any other region of the *Address correspondence to Dr. Kazue Uchida, Virus Division, Saitama Institute of Public Health, Kamiokubo 639-1, Saitama, Saitama, 338-0824, Japan.…”

mentioning

confidence: 99%

“…Fax: +81-48-840-1041. E-mail: virus31 @f3.dion.ne.jp 851 MuV genome; therefore it is useful for the identification and classification ofMuV isolates (12)(13)(14). Orvell et al analyzed the SH gene nucleotide sequences of MuV isolates from USA, Europe, and Japan and suggested that these strains formed five genotypes A to E (8).…”

mentioning

confidence: 99%

Characterization of Mumps Virus Isolated in Saitama Prefecture, Japan, by Sequence Analysis of the SH Gene

Uchida¹,

Shinohara²,

Shimada³

et al. 2001

Microbiology and Immunology

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Mumps virus (MuV) strains isolated from cerebrospinal fluid and throat swabs from patients in Saitama Prefecture and Tokyo, Japan, from 1997 to 2000 were examined by analyzing the SH gene nucleotide sequence (316-nt). Eighteen of the 20 strains studied were divided into three genotypes, recognized as B, G, and H in previous reports. Two genotypes (G and H) are believed to be new in Japan. Two of the 20 strains belonged to none of the previously reported genotypes (A-I), but were closely related to two known strains, MP94-H and Lougl/UK97. We propose that the two strains identified in this study together with the previously reported strains, MP94-H and Lougl/UK97, form a new genotype, designated J, based on the divergence of the SH gene nucleotide sequences between these four strains and other strains reported (genotypes A-I). Our results also suggest that more than two genotypes circulated in Saitama Prefecture from 1997 to 1999, but only one, genotype G, was in evidence in 2000. Genotype B was earlier reported as the predominant strain in Japan, but it became undetectable by the year 2000. These results provide important epidemiological data on mumps in Japan.

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“…F and HN, integral membrane proteins which project from the surface of the virion, are involved in virus attachment and entry of cells. The SH and M proteins are also membrane associated (18,38).…”

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confidence: 99%

Rescue of Mumps Virus from cDNA

Clarke

Sidhu

Johnson

et al. 2000

J Virol

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A complete DNA copy of the genome of a Jeryl Lynn strain of mumps virus (15,384 nucleotides) was assembled from cDNA fragments such that an exact antigenome RNA could be generated following transcription by T7 RNA polymerase and cleavage by hepatitis delta virus ribozyme. The plasmid containing the genome sequence, together with support plasmids which express mumps virus NP, P, and L proteins under control of the T7 RNA polymerase promoter, were transfected into A549 cells previously infected with recombinant vaccinia virus (MVA-T7) that expressed T7 RNA polymerase. Rescue of infectious virus from the genome cDNA was demonstrated by amplification of mumps virus from transfected-cell cultures and by subsequent consensus sequencing of reverse transcription-PCR products generated from infected-cell RNA to verify the presence of specific nucleotide tags introduced into the genome cDNA clone. The only coding change (position 8502, A to G) in the cDNA clone relative to the consensus sequence of the Jeryl Lynn plaque isolate from which it was derived, resulting in a lysine-to-arginine substitution at amino acid 22 of the L protein, did not prevent rescue of mumps virus, even though an amino acid alignment for the L proteins of paramyxoviruses indicates that lysine is highly conserved at that position. This system may provide the basis of a safe and effective virus vector for the in vivo expression of immunologically and biologically active proteins, peptides, and RNAs.

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The Mumps Virus SH Protein Is a Membrane Protein and Not Essential for Virus Growth

Cited by 86 publications

References 3 publications

Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)

Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)

Characterization of Mumps Virus Isolated in Saitama Prefecture, Japan, by Sequence Analysis of the SH Gene

Rescue of Mumps Virus from cDNA

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