Protein cleavage and poxvirus morphogenesis: Tryptic peptide analysis of core precursors accumulated by blocking assembly with rifampicin

Moss, Bernard; Rosenblum, Edith N.

doi:10.1016/0022-2836(73)90195-2

Cited by 125 publications

(92 citation statements)

References 17 publications

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“…Unlike P4a and P4b, the apparent size of the P25K protein is in close agreement with its predicted Mr. The relationships between the core proteins and their precursors have previously been established by tryptic peptide mapping, pulse-chase analysis and immunological assays (Katz & Moss, 1970a, b;Moss & Rosenblum, 1973;Rosel & Moss, 1985;Sarov & Joklik, 1972;Weir & Moss, 1985;Yang et al, 1988). The cleavage of the P4a, P4b and P25K precursor proteins during VV morphogenesis is apparently an obligatory reaction, because drugs that inhibit cleavage, either directly or indirectly [e.g.…”

supporting

confidence: 69%

Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins

VanSlyke

Franke²,

Hruby³

1991

Journal of General Virology

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supporting

confidence: 69%

Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins

VanSlyke

Franke²,

Hruby³

1991

Journal of General Virology

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“…The roles of abundant proteins are assumed to be structural although they may have additional roles. The precursors of some major core proteins are proteolytically processed during the assembly of vaccinia virus particles (43). One of these, P4A, encoded by the A10L ORF (44,45), can interact with itself in the two-hybrid system.…”

Section: Virion Structural͞morphogenesis Proteinsmentioning

confidence: 99%

Genome-wide analysis of vaccinia virus protein–protein interactions

McCraith

Holtzman²,

Moss³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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266

205

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To detect interactions between proteins of vaccinia virus, we carried out a comprehensive two-hybrid analysis to assay every pairwise combination. We constructed an array of yeast transformants that contained each of the 266 predicted viral ORFs as Gal4 activation domain hybrid proteins. The array was individually mated to transformants containing each ORF as a Gal4 -DNAbinding domain hybrid, and diploids expressing the two-hybrid reporter gene were identified. Of the Ϸ70,000 combinations, we found 37 protein-protein interactions, including 28 that were previously unknown. In some cases, e.g., late transcription factors, both proteins were known to have related roles although there was no prior evidence of physical associations. For some other interactions, neither protein had a known role. In the majority of cases, however, one of the interacting proteins was known to be involved in DNA replication, transcription, virion structure, or host evasion, thereby providing a clue to the role of the other uncharacterized protein in a specific process.

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“…In connection with this, it should be mentioned that other complex DNA-containing viruses, such as adenoviruses and poxviruses, use proteolytic processing at similar or identical cleavage sequences for the maturation of major core proteins. In the case of poxviruses, the cleavage of core precursors is crucial for the formation of virus particles, which does not take place if the processing is blocked (36). In contrast, the adenovirus protease acts in newly assembled virions, being needed for their maturation into infectious virions (37).…”

Section: Characterization Of Protein Ps273r As a Cysteine Protease-asmentioning

confidence: 99%

African Swine Fever Virus Protease, a New Viral Member of the SUMO-1-specific Protease Family

Andrés¹,

Alejo²,

Simón‐Mateo³

et al. 2001

Journal of Biological Chemistry

107

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African swine fever virus (ASFV) is a complex DNA virus that employs polyprotein processing at Gly-GlyXaa sites as a strategy to produce several major core components of the viral particle. The virus gene S273R encodes a 31-kDa protein that contains a "core domain" with the conserved catalytic residues characteristic of SUMO-1-specific proteases and the adenovirus protease. Using a COS cell expression system, it was found that protein pS273R is capable of cleaving the viral polyproteins pp62 and pp220 in a specific way giving rise to the same intermediates and mature products as those produced in ASFV-infected cells. Furthermore, protein pS273R, like adenovirus protease and SUMO-1-specific enzymes, is a cysteine protease, because its activity is abolished by mutation of the predicted catalytic histidine and cysteine residues and is inhibited by sulfhydryl-blocking reagents. Protein pS273R is expressed late after infection and is localized in the cytoplasmic viral factories, where it is found associated with virus precursors and mature virions. In the virions, the protein is present in the core shell, a domain where the products of the viral polyproteins are also located. The identification of the ASFV protease will allow a better understanding of the role of polyprotein processing in virus assembly and may contribute to our knowledge of the emerging family of SUMO-1-specific proteases.Positive strand RNA viruses and retroviruses encode polyproteins, which are proteolytically cleaved by viral proteases to yield the nonstructural and structural proteins required for replication and morphogenesis (1-3). On the other hand, DNA viruses, such as adenoviruses and poxviruses, synthesize precursor proteins whose maturation by proteolytic removal of terminal peptides plays an essential role in virion formation (1).African swine fever virus (ASFV), 1 a large and complex virus containing a 170-kb double-stranded DNA molecule with 151 potential genes (4, 5), is atypical among DNA viruses in that it encodes two polyproteins, pp220 and pp62, which are cleaved to produce six major structural components of the virus particle (6, 7). These proteins, p150, p37, p34, and p14, derived from polyprotein pp220 and p35 and p15, products of polyprotein pp62, are the major components of the core shell, a thick protein layer that surrounds the DNA-containing central nucleoid and that is enwrapped by the inner lipoprotein envelope and the icosahedral capsid (8).2 All the proteolytic cleavages occur after the second Gly of the consensus sequence Gly-GlyXaa, which is also recognized as a cleavage site in the maturation of adenovirus structural proteins and in some cellular proteins, including polyubiquitin (9) and ubiquitin-like proteins (10). A similar cleavage site (Ala-Gly-Xaa) is used for the maturation of vaccinia virus structural proteins (11,12). Although the adenovirus protease that processes at Gly-Gly-Xaa sites is well characterized (13-15), the enzymes involved in the processing of the ASFV polyproteins or in the cleavage of vaccin...

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Protein cleavage and poxvirus morphogenesis: Tryptic peptide analysis of core precursors accumulated by blocking assembly with rifampicin

Cited by 125 publications

References 17 publications

Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins

Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins

Genome-wide analysis of vaccinia virus protein–protein interactions

African Swine Fever Virus Protease, a New Viral Member of the SUMO-1-specific Protease Family

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