Polypeptides and structure of African swine fever virus

Schloer, G. M.

doi:10.1016/0168-1702(85)90431-9

Cited by 21 publications

(14 citation statements)

References 21 publications

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“…The infectivity of intracellular vE120Ri particles is consistent with early work showing that preparations of partially purified cell-associated ASFV particles are infectious (42), that the outer viral envelope is not necessary for infectivity (42), and that antibodies against the capsid protein p72 can neutralize ASFV infection (7,28). Unlike extracellular virions (12), intracellular mature particles have not been efficiently purified so far mainly due to their high contamination with cellular membranes as well as extracellular particles, which often lose the outer envelope (42).…”

Section: Discussionsupporting

confidence: 69%

“…Unlike extracellular virions (12), intracellular mature particles have not been efficiently purified so far mainly due to their high contamination with cellular membranes as well as extracellular particles, which often lose the outer envelope (42). In relation to this, the recombinant vE120Ri can be a useful tool to purify intracellular ASFV mature particles and to establish the differences in composition and infectivity with the extracellular enveloped particles.…”

Section: Discussionmentioning

confidence: 99%

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African Swine Fever Virus Structural Protein pE120R Is Essential for Virus Transport from Assembly Sites to Plasma Membrane but Not for Infectivity

Andrés

García‐Escudero

Viñuela

et al. 2001

J Virol

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This report examines the role of African swine fever virus (ASFV) structural protein pE120R in virus replication. Immunoelectron microscopy revealed that protein pE120R localizes at the surface of the intracellular virions. Consistent with this, coimmunoprecipitation assays showed that protein pE120R binds to the major capsid protein p72. Moreover, it was found that, in cells infected with an ASFV recombinant that inducibly expresses protein p72, the incorporation of pE120R into the virus particle is dependent on p72 expression. Protein pE120R was also studied using an ASFV recombinant in which E120R gene expression is regulated by the Escherichia coli lac repressor-operator system. In the absence of inducer, pE120R expression was reduced about 100-fold compared to that obtained with the parental virus or the recombinant virus grown under permissive conditions. One-step virus growth curves showed that, under conditions that repress pE120R expression, the titer of intracellular progeny was similar to the total virus yield obtained under permissive conditions, whereas the extracellular virus yield was about 100-fold lower than in control infections. Immunofluorescence and electron microscopy demonstrated that, under restrictive conditions, intracellular mature virions are properly assembled but remain confined to the replication areas. Altogether, these results indicate that pE120R is necessary for virus dissemination but not for virus infectivity. The data also suggest that protein pE120R might be involved in the microtubule-mediated transport of ASFV particles from the viral factories to the plasma membrane.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionmentioning

confidence: 99%

African Swine Fever Virus Structural Protein pE120R Is Essential for Virus Transport from Assembly Sites to Plasma Membrane but Not for Infectivity

Andrés

García‐Escudero

Viñuela

et al. 2001

J Virol

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“…Approximately 100 virus-induced proteins of 10-220 kDa can be detected in infected cells, including about twice as many late proteins as early proteins (Escribano and Tabares 1987;Estevez et al 1986;Rodriguez et al 2001;Santaren and Viñuela 1986;Tabares et al 1980bTabares et al , 1983Urzainqui et al 1987). More than 50 structural proteins of 11.5-150 kDa can be detected in purified virions by 2D gel electrophoresis, with one-to two-thirds as many detected in 1D gels (Carrascosa et al 1985;Estevez et al 1986;Schloer 1985;Tabares et al 1980a). While viral proteins are often localized to viral factories, other patterns of expression have been observed, including nuclear, diffuse cytoplasmic, and cellular membrane staining using monoclonal antibodies or the presence of viral proteins in nuclear cell fractions (Sanz et al 1985;Tabares et al 1980bTabares et al , 1983.…”

Section: Protein Synthesis and Modificationmentioning

confidence: 96%

“…The ASFV virion is comprised of more than 50 polypeptides and has a complex but regular structure by electron microscopy, icosahedral in symmetry and containing several concentric layers for an overall diameter of approximately 200 nm (Breese and DeBoer 1966;Carrascosa et al 1984Carrascosa et al , 1985Estevez et al 1986;Schloer 1985) ( Fig. 1 A).…”

Section: Asfv Virionmentioning

confidence: 97%

African Swine Fever Virus

Tulman

Delhon

et al. 2009

Current Topics in Microbiology and Immunology

135

117

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African swine fever virus (ASFV) is a large, intracytoplasmicallyreplicating DNA arbovirus and the sole member of the family Asfarviridae . It is the etiologic agent of a highly lethal hemorrhagic disease of domestic swine and therefore extensively studied to elucidate the structures, genes, and mechanisms affecting viral replication in the host, virus-host interactions, and viral virulence. Increasingly apparent is the complexity with which ASFV replicates and interacts with the host cell during infection. ASFV encodes novel genes

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“…More than 100 proteins are induced in ASFV-infected cells and extracellular virions contain more than 50 proteins, although none of these are major * Author for correspondence. Fax +44 1483 232448. e-mail linda.dixon@BBSRC.ac.uk structural glycoproteins (Carvalho & RodriguesPousada, 1986;Esteves et al, 1986;Schloer, 1985;Del Val et al, 1986;Del Val & Vifiuela, 1987). Only a few structural proteins have been mapped to specific genes on the virus genome.…”

Section: Introductionmentioning

confidence: 99%

African swine fever virus gene j13L encodes a 25-27 kDa virion protein with variable numbers of amino acid repeats

Sun

Jacobs

Smith

et al. 1995

Journal of General Virology

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The African swine fever virus (ASFV)j 13L gene encodes a 177 amino acid protein (19.0 kDa) with a putative transmembrane domain between residues 32 and 52. There is a potential signal peptide cleavage site at residue 54 and several possible motifs for phosphorylation and myristylation. Rabbit antisera raised against a synthetic peptide from the C terminus of the j 13L ORF identified proteins of 25-27 kDa in cells infected with a recombinant vaccinia virus expressing the j 13L ORF, in ASFV-infected cells and in purified extracellular ASF virions. In ASFV-infected cells the jl3L protein was expressed late during infection and exhibited size variation (25-27 kDa) between the different ASFV strains. Nucleotide sequence analysis of the gene in these strains showed that these size differences were due to variation in the number and sequence of tandemly repeated amino acid repeats. Although ASFV-infected animals made antibodies to the jl3L protein, no protection was observed when pigs were vaccinated with a recombinant vaccinia virus expressing the j 13L ORF.

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Polypeptides and structure of African swine fever virus

Cited by 21 publications

References 21 publications

African Swine Fever Virus Structural Protein pE120R Is Essential for Virus Transport from Assembly Sites to Plasma Membrane but Not for Infectivity

African Swine Fever Virus Structural Protein pE120R Is Essential for Virus Transport from Assembly Sites to Plasma Membrane but Not for Infectivity

African Swine Fever Virus

African swine fever virus gene j13L encodes a 25-27 kDa virion protein with variable numbers of amino acid repeats

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