Inhibition of cellular protein synthesis by vaccinia virus surface tubules

Mbuy, Gustave K.N.; Morris, Randal E.; Bubel, H. Curt

doi:10.1016/0042-6822(82)90409-3

Cited by 15 publications

(12 citation statements)

References 37 publications

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“…Proteins at 87K, 73K, 67K, 61K and 57K were found only in the core corresponding to the major core proteins described by Essani & Dales (1979) and Oie & Ichihashi (1981). Additionally, three proteins at 32K, 30K and 14K were found; the latter may be identical to a 13.8K core protein (Ichihashi et al, 1982), but it is well known that incubation of vaccinia virus with detergents does not completely remove tubules from the cores (Mbuy et al, 1982) which would result in tubule-specific antibodies after immunization with such a preparation. Orthopoxviruses have .been standardized mainly by biological characteristics and DNA analysis.…”

Section: Discussionmentioning

confidence: 99%

“…Oie & Ichihashi (1987) described neutralizing MAbs binding to virus proteins at 54K, 34K, 32K, 29K and 25K to 17K which could be extracted from the envelope by NP40 and mercaptoethanol (Ichihashi & Oie, 1980;Oie & Ichihashi, 1981). Stern & Dales (1976) isolated a 58K surface tubule protein that induced cell--cell fusion and neutralizing antibodies in rabbit sera which inhibited cellular protein synthesis (Mbuy et al, 1982) and which was identical to the 54K protein of Oie & Ichihashi (1981). It is difficult to compare M, data for apparently homologous polypeptides from several authors, because different techniques were used which led to slight variations in the values.…”

Section: Discussionmentioning

confidence: 99%

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Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Czerny¹,

Mahnel²

1990

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Czerny¹,

Mahnel²

1990

Journal of General Virology

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“…Herpesviruses utilize the virion-associated, viral host shutoff (VHS) protein to inhibit protein synthesis (25). A number of competing mechanisms, including the virion surface tubule protein, have been proposed for host shutoff in poxvirus infections (1,15,32,35).…”

Section: Discussionmentioning

confidence: 99%

A Virion-Associated Protein Kinase Induces Apoptosis

Chitnis¹,

Paul

Lawrence

et al. 2011

J Virol

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Apoptosis and inhibition of host gene expression are often associated with virus infections. Many viral polypeptides modulate apoptosis by direct interaction with highly conserved apoptotic pathways. Some viruses induce apoptosis during late stages of the infection cycle, while others inhibit apoptosis to facilitate replication or maintain persistent infection. In previous work, we showed that Chilo iridescent virus (CIV) or CIV virion protein extract induces apoptosis in spruce budworm and cotton boll weevil cell cultures. Here, we characterize the product of a CIV gene (iridovirus serine/threonine kinase; istk) with signature sequences for S/T kinase and ATP binding. ISTK appears to belong to the superfamily, vaccinia-related kinases (VRKs). The istk gene was expressed in Pichia pastoris vectors. Purified ISTK (48 kDa) exhibited S/T kinase activity. Treatment with ISTK induced apoptosis in budworm cells. A 35-kDa cleavage product of ISTK retaining key signature sequences was identified during purification. Pichia-expressed 35-kDa polypeptide, designated iridoptin, induced apoptosis and inhibition of host protein synthesis in budworm and boll weevil cells. A mutation in the ATP-binding site eliminated both kinase and apoptosis activity of iridoptin, suggesting that kinase activity is essential for induction of apoptosis. Analysis with custom antibody confirmed that ISTK is a structural component of CIV particles. This is the first demonstration of a viral kinase inducing apoptosis in any virus-host system and the first identification of a factor inducing apoptosis or host protein shutoff for the family Iridoviridae.

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“…In fact, several hours after infection, viral transcripts account for most of the mRNA in the cytoplasm of the infected cell (Boone and Moss, 1978;Cooper and Moss, 1979). In addition, direct effects on translation have been assigned to virion proteins (Mbuy et al, 1982;PersonFernández and Beaud, 1986;Beaud et al, 1994), early proteins Dru, 1980), or RNAs (RosemondHornbeak andMoss, 1975;Gershowitz and Moss, 1979). Vaccinia late mRNAs are similar to cellular mRNAs in several ways; they are capped and polyadenilated.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, a variety of cellular proteins and RNAs have been implicated in regulating the translation of viral versus cellular mRNAs. For instance, small RNAs (Bablanian et al, 1978;Bablanian et al, 1993;Cacoullos and Bablanian, 1993), the surface tubules of the virus particle (Mbuy et al, 1982), or the proteins F17R (Person-Fernández and Beaud, 1986) and B1R (Beaud et al, 1994) have been proposed as specific inhibitors of host protein synthesis.…”

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confidence: 99%

AUG context and mRNA translation in vaccinia virus

Sánchez-Puig¹,

Blasco²

2008

Span. j. agric. res.

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In this study, we examined the role of the nucleotides flanking AUG initiator codons in modulating translation of vaccinia virus genes. First, the sequence around initiation codons in the genomic sequence of vaccinia was analyzed. A preference for A in position 3 and for A or G in position +4, relative to the A of the initiator AUG codon was noted. These results are in broad agreement with known optimal consensus for the translation of eukaryotic mRNAs. Nucleotides 3 and +4, which are known to affect the efficiency of translation of cellular mRNAs over a 20-fold range, were examined by site-directed mutagenesis and functional assays in the context of vaccinia-infected cells. A collection of virus recombinants expressing beta-Galactosidase (beta-Gal) under the control of a strong promoter and containing all possible nucleotide substitutions in those positions was generated. Quantitation of beta-Gal mRNA and beta-Gal activity showed that the efficiency of translation was not affected significantly by nucleotide substitutions in positions 3 and +4. Therefore, despite the high occurrence of purine nucleotides in those positions in vaccinia mRNAs, no effect of those positions was noted in conditions where â-Gal was overexpressed.

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Inhibition of cellular protein synthesis by vaccinia virus surface tubules

Cited by 15 publications

References 37 publications

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

A Virion-Associated Protein Kinase Induces Apoptosis

AUG context and mRNA translation in vaccinia virus

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