African Swine Fever Virus EP153R Open Reading Frame Encodes a Glycoprotein Involved in the Hemadsorption of Infected Cells

Galindo, Inmaculada; Almazán, Fernando; Bustos, María José; Viñuela, Eladio; Carrascosa, Ángel L.

doi:10.1006/viro.1999.0080

Cited by 75 publications

(55 citation statements)

References 31 publications

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“…pA224L inhibited caspase activity and cell death induced by various means when stably overexpressed in Vero cells, an effect likely resulting from the direct interaction of pA224L with the catalytic fragment of caspase-3 (Nogal et al 2001). Caspase-3 activity is also affected by ASFV pEP153R, a C-type lectin-like protein expressed throughout the infectious cycle (Galindo et al 2000a;Yanez 1995). Increased levels of caspase-3 and apoptosis occurred in cells infected with ASFV mutants lacking EP153R (Hurtado et al 2004).…”

Section: Viral Modulation Of Apoptosismentioning

confidence: 98%

African Swine Fever Virus

Tulman

Delhon

et al. 2009

Current Topics in Microbiology and Immunology

132

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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Section: Viral Modulation Of Apoptosismentioning

confidence: 98%

African Swine Fever Virus

Tulman

Delhon

et al. 2009

Current Topics in Microbiology and Immunology

132

117

View full text Add to dashboard Cite

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“…This ASFV protein is required for the hemadsorption (HAD) of red blood cells around ASFV-infected cells and also for the association of extracellular virions with red blood cells (5,23,26). One report showed that deleting the ORF EP153R, which encodes a C-type lectin, reduced the numbers of red blood cells binding to infected cells, suggesting that EP153R was also involved in HAD (13). Although most isolates of ASFV cause HAD, some field isolates that are non-HAD have been characterized, and these include both virulent and nonvirulent isolates (4,20,30).…”

mentioning

confidence: 99%

Processing and Localization of the African Swine Fever Virus CD2v Transmembrane Protein

Goatley

Dixon

2011

J Virol

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The African swine fever virus (ASFV)-encoded CD2v transmembrane protein is required for the hemadsorption of red blood cells around infected cells and is also required for the inhibition of bystander lymphocyte proliferation in response to mitogens. We studied the expression of CD2v by expressing the gene with a V5 tag downstream from the signal peptide near the N terminus and a hemagglutinin (HA) tag at the C terminus. In ASFV-infected cells, a full-length glycosylated form of the CD2v protein, which migrated mainly as a 89-kDa product, was detected, as well as an N-terminal glycosylated fragment of 63 kDa and a C-terminal nonglycosylated fragment of 26 kDa. All of these forms of the protein were localized in the membrane fraction of cells. The 26-kDa C-terminal fragment was also produced in infected cells treated with brefeldin A. These data indicate that the CD2v protein is cleaved within the luminal domain and that this occurs in the endoplasmic reticulum or Golgi compartments. Confocal microscopy showed that most of the expressed CD2v protein was localized within cells rather than at the cell surface. Comparison of the localization of full-length CD2v with that of a deletion mutant lacking all of the cytoplasmic tail apart from the 12 membrane-proximal amino acids indicated that signals within the cytoplasmic tail are responsible for the predominant localization of the full-length and C-terminal 26-kDa fragment within membranes around the virus factories, which contain markers for the Golgi compartment. Processing of the CD2v protein was not observed in uninfected cells, indicating that it is induced by ASFV infection.

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“…The principal exception to this is the product of the EP402R gene, which is a viral homologue of CD2 and, in conjunction with the product of the EP135R gene, recruits erythrocytes to infected cells. This may sterically mask virally infected cells from cytotoxic white blood cells (5,12,33). ASFV also encodes an inhibitor of nuclear factor B (NF-B) and nuclear factor of activated T cells, which can repress proinflammatory immune responses (25,29,36).…”

mentioning

confidence: 99%

African Swine Fever Virus Causes Microtubule-Dependent Dispersal of the trans -Golgi Network and Slows Delivery of Membrane Protein to the PlasmaMembrane

Netherton

McCrossan

Denyer

et al. 2006

J Virol

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Viral interference with secretory cargo is a common mechanism for pathogen immune evasion. Selective down regulation of critical immune system molecules such as major histocompatibility complex (MHC) proteins enables pathogens to mask themselves from their host. African swine fever virus (ASFV) disrupts the trans-Golgi network (TGN) by altering the localization of TGN46, an organelle marker for the distal secretory pathway. Reorganization of membrane transport components may provide a mechanism whereby ASFV can disrupt the correct secretion and/or cell surface expression of host proteins. In the study reported here, we used the tsO45 temperature-sensitive mutant of the G protein of vesicular stomatitis virus to show that ASFV significantly reduces the rate at which the protein is delivered to the plasma membrane. This is linked to a general reorganization of the secretory pathway during infection and a specific, microtubule-dependent disruption of structural components of the TGN. Golgin p230 and TGN46 are separated into distinct vesicles, whereupon TGN46 is depleted. These data suggest that disruption of the TGN by ASFV can slow membrane traffic during viral infection. This may be functionally important because infection of macrophages with virulent isolates of ASFV increased the expression of MHC class I genes, but there was no parallel increase in MHC class I molecule delivery to the plasma membrane.

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African Swine Fever Virus EP153R Open Reading Frame Encodes a Glycoprotein Involved in the Hemadsorption of Infected Cells

Cited by 75 publications

References 31 publications

African Swine Fever Virus

African Swine Fever Virus

Processing and Localization of the African Swine Fever Virus CD2v Transmembrane Protein

African Swine Fever Virus Causes Microtubule-Dependent Dispersal of the trans -Golgi Network and Slows Delivery of Membrane Protein to the PlasmaMembrane

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