Analysis of the Complete Nucleotide Sequence of African Swine Fever Virus

Yáñez, R. J.; Rodrı́guez, Javier M.; Nogal, Marı́a L.; Yuste, Luís; Enrı́quez, Carlos; Rodrı́guez, José F.; Viñuela, Eladio

doi:10.1006/viro.1995.1149

Cited by 400 publications

(263 citation statements)

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“…However, the architecture of the MCP gene of faustovirus is clearly different from the asfaviruses and other nucleocytoplasmic large dsDNA viruses (NCLDVs).The gene that encodes the MCP in asfarvirus, B646L, is in the form of a single fragment of 1,941 bp (3,4). In faustovirus, the genomic organization of the MCP gene is novel and, to our knowledge, unique in the virus world.…”

Section: Genomic Organization Of the Faustovirus Mcp Genementioning

confidence: 99%

Structure of faustovirus, a large dsDNA virus

Klose

Reteno

Benamar

et al. 2016

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

117

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International audienceMany viruses protect their genome with a combination of a protein shell with or without a membrane layer. Here we describe the structure of faustovirus, the first DNA virus (to our knowledge) that has been found to use two protein shells to encapsidate and protect its genome. The crystal structure of the major capsid protein, in combination with cryo-electron microscopy structures of two different maturation stages of the virus, shows that the outer virus shell is composed of a double jelly-roll protein that can be found in many double-stranded DNA viruses. The structure of the repeating hexameric unit of the inner shell is different from all other known capsid proteins. In addition to the unique architecture, the region of the genome that encodes the major capsid protein stretches over 17,000 bp and contains a large number of introns and exons. This complexity might help the virus to rapidly adapt to new environments or hosts

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Section: Genomic Organization Of the Faustovirus Mcp Genementioning

confidence: 99%

Structure of faustovirus, a large dsDNA virus

Klose

Reteno

Benamar

et al. 2016

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

117

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“…Previous RFLP studies of 17 viruses recovered from outbreaks in Malawi between 1982 and 1989 confirmed the presence of a central variable region (CVR) within the central 125 kb conserved region of the genome [5]. This length variation was subsequently shown to result from differences openUP (December 2007) in a tetrameric repeat region located within the late viral gene, 9RL [6], also termed the B602L gene [7,8]. The protein, which varies in size in accordance with the number of repeats within the CVR is homogeneously distributed throughout the cytoplasm and is strongly recognised by convalescent swine serum [6].…”

Section: Introductionmentioning

confidence: 98%

Intra-genotypic resolution of African swine fever viruses from an East African domestic pig cycle: a combined p72-CVR approach

et al. 2007

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Two of the 22 presently recognised African swine fever (ASF) virus p72 genotypes are genetically homogeneous and are associated with domestic pig cycles. Of these, genotype VIII comprises just two p72 variants, designated 'a' and 'b' in this study, and is confined four or less viruses with a maximum circulation period of three years. A combined p72-CVR analysis resulted in eight discrete lineages corresponding to eight unique p72-CVR combinations. One of these, b-F, appears to have arisen by convergent evolution or through an intra-genotypic recombination event, as the individual p72 and CVR gene phylogenies are incongruent. This raises the possibility of intra-genotypic recombination in ASF viruses for the first time. However, given the repetitive nature of the CVR region, convergent evolution cannot be excluded and may be the more likely explanation.

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“…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).…”

mentioning

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

104

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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Analysis of the Complete Nucleotide Sequence of African Swine Fever Virus

Cited by 400 publications

References 0 publications

Structure of faustovirus, a large dsDNA virus

Structure of faustovirus, a large dsDNA virus

Intra-genotypic resolution of African swine fever viruses from an East African domestic pig cycle: a combined p72-CVR approach

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

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