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

Goatley, Lynnette; Dixon, Linda K.

doi:10.1128/jvi.01994-10

Cited by 59 publications

(67 citation statements)

References 29 publications

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“…In contrast, the analysis of the EP402R gene revealed some differences in the number of TRS. The CD2v transmembrane protein, similar to the host T‐cell adhesion molecule CD2 (Dixon et al., ; Goatley and Dixon, ), is required for haemadsorption of red blood cells around infected macrophages and for the adhe‘sion of extracellular virions to erythrocytes and consequent viral dissemination. Expression of the CD2v protein enhances virus replication in the tick vector Ornithodoros erraticus (Rowlands et al., ).…”

Section: Discussionmentioning

confidence: 99%

Improved Strategy for Molecular Characterization of African Swine Fever Viruses from Sardinia, Based on Analysis of p30, CD2V and I73R /I329L Variable Regions

Sanna

Giudici

Bacciu

et al. 2016

Transbound Emerg Dis

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African swine fever virus (ASFV) is the aetiological agent of a highly lethal haemorrhagic disease affecting pigs that inflicts significant economic damage on the swine industry. ASF is present in many African countries, in several eastern and central European countries and in Sardinia (Italy). Sequence analyses of variable genomic regions have been extensively used for molecular epidemiological studies of ASFV isolates. Previous sequencing data of genes that codify for viral protein p54, p72 and the central variable region (CVR) within the B602L gene revealed that Sardinian isolates show a very low level of variability. To achieve a finer level of discrimination among such closely related viruses, in this study, we have chosen three different genome regions to investigate the within-genotype relationships and to provide a more accurate assessment of the origin of outbreaks. The analysis of p30 and I73R/I329L sequences obtained from ASFV collected in Sardinia over a 13-years period confirms a remarkable genetic stability in these regions. The sequence comparison of the protein encoded by the EP402R gene (CD2v), carried out on various strains from 1978 to 2014, revealed a temporal subdivision of Sardinian viruses into two subgroups: one group includes the historical isolates from 1978 to 1990, and the second one is comprised of the viruses collected from 1990 until 2014. These data, together with those obtained from CVR within the B602L gene analysis, demonstrated that the viruses circulating in Sardinia belong to p72 genotype I, but have undergone genetic variations in two different regions of the genome since 1990. We proposed the cytoplasmic region of CD2v protein as a new genetic marker that could be use to analyse ASFVs from different locations to track virus spread. Our study reaffirms the need to analyse other genome regions in order to improve the molecular characterization of ASFV.

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Section: Discussionmentioning

confidence: 99%

Improved Strategy for Molecular Characterization of African Swine Fever Viruses from Sardinia, Based on Analysis of p30, CD2V and I73R /I329L Variable Regions

Sanna

Giudici

Bacciu

et al. 2016

Transbound Emerg Dis

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“…Protein pEP402R has been shown to be responsible for the adhesion of erythrocytes to infected cells and for the binding of ASFV particles to erythrocytes. Intriguingly, it has been localized to the Golgi network around the virus factories but not at the cell surface (47,50). To ascertain the subviral localization of membrane proteins p22 and pEP402R, we performed immunogold labeling on cryosections of ASFV-infected cells.…”

Section: Figmentioning

confidence: 99%

A Proteomic Atlas of the African Swine Fever Virus Particle

Alejo

Matamoros

Guerra

et al. 2018

J Virol

304

310

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African swine fever virus (ASFV) is a large and complex DNA virus that causes a highly lethal swine disease for which there is no vaccine available. The ASFV particle, with an icosahedral multilayered structure, contains multiple polypeptides whose identity is largely unknown. Here, we analyzed by mass spectroscopy the protein composition of highly purified extracellular ASFV particles and performed immunoelectron microscopy to localize several of the detected proteins. The proteomic analysis identified 68 viral proteins, which account for 39% of the genome coding capacity. The ASFV proteome includes essentially all the previously described virion proteins and, interestingly, 44 newly identified virus-packaged polypeptides, half of which have an unknown function. A great proportion of the virion proteins are committed to the virus architecture, including two newly identified structural proteins, p5 and p8, which are derived from the core polyproteins pp220 and pp62, respectively. In addition, the virion contains a full complement of enzymes and factors involved in viral transcription, various enzymes implicated in DNA repair and protein modification, and some proteins concerned with virus entry and host defense evasion. Finally, 21 host proteins, many of them localized at the cell surface and related to the cortical actin cytoskeleton, were reproducibly detected in the ASFV particle. Immunoelectron microscopy strongly supports the suggestion that these host membrane-associated proteins are recruited during virus budding at actin-dependent membrane protrusions. Altogether, the results of this study provide a comprehensive model of the ASFV architecture that integrates both compositional and structural information. African swine fever virus causes a highly contagious and lethal disease of swine that currently affects many countries of sub-Saharan Africa, the Caucasus, the Russian Federation, and Eastern Europe and has very recently spread to China. Despite extensive research, effective vaccines or antiviral strategies are still lacking, and many basic questions on the molecular mechanisms underlying the infective cycle remain. One such gap regards the composition and structure of the infectious virus particle. In the study described in this report, we identified the set of viral and host proteins that compose the virion and determined or inferred the localization of many of them. This information significantly increases our understanding of the biological and structural features of an infectious African swine fever virus particle and will help direct future research efforts.

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“…The extracellular domain CD2v is similar to that of the host CD2 binding protein and contains two Ig-like domains and 15 potential sites for N-glycolization unlike 3-4 in CD2 [48,50,51]. The molecular weight of the full-size glycosylated CD2v in the isolate Malawi LIL20/1 is 105-110 kDa [52]. In the absence of gene encoding CD2v protein in the virulent ASFV genome impeded the viremia and dissemination of the virus in swine body, but did not reduce the death from the virus.…”

Section: Vpmentioning

confidence: 99%

THE HAEMADSORPTION AT AFRICAN SWINE FEVER (review)

Sereda¹,

Imatdinov²,

Makarov³

2016

S-h. biol.

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A b s t r a c tThe capability of causing haemadsorption at African swine fever (ASF) virus (ASFV) reproduction in swine bone marrow cell cultures, leukocytes or continuous cells in the presence of swine erythrocytes is characteristic of the majority of the virus isolates (W.A. Malmquist, D. Hay, 1960). This trait is used for ASF diagnosis based on autohaemadsorption in porcine blood, the virus titration in cell culture, and selection of its attenuated variants in vitro (A.D. Sereda et al., 2014). The haemadsorption inhibition assay (HIA) in tandem with the bioassay using the disease-resistant pigs is applied for seroimmunotype-based classification of ASFV isolates (N.I. Mitin et al., 1985). The heterogeneity of an ASFV population for quantitative haemadsorption characteristic (like «dense», «moderate» or «loose») is a phenotypic trait of ASFV isolates, strains and/or variants (V. Makarov et al., 2016). Also, the proportion of the circumference of red blood cells as observed at their contact with infected macrophages serves as another quantifiable feature of haemadsorption. Some quantitative differences in HIA activity levels of swine blood sera are determined in the assays carried out using virulent reference variants and their attenuated derivatives, and the obtained results require some interpretation. The loss of ability to induce haemadsorption is not critical for ASFV reproduction and often accompanied by a decrease in the pathogen virulence levels. Hence, as a rule, attenuated ASFV variants are prepared through a selection by limiting dilution from populations of virulent isolates of the virus clones that are characterized by a reduced potential to induce haemadsorption (D.V. Kolbasov et al., 2014). In the course of the virus reproduction, haemadsorption precedes the exocytosis. Virions do not play a significant role in the mechanism of haemadsorption, nevertheless, their interaction with erythrocyte membranes promotes the virus dissemination throughout the swine organism and more effective introduction into the gut cells of ticks (L.K. Dixon et al., 2004). ASFV haemadsorbing potentiality is determined by highly glycosylated transmembrane protein CD2v (J.M. Rodríguez et al., 1993). Probably, nonhaemadsorbing avirulent isolates emerge as a result of some shift of the open reading frames for EP402R and EP153R encoding the CD2v and lectin-like proteins, respectively (D. A. Chapman et al., 2008). An assumption is made that the haemadsorption phenomenon is due to an interaction between carbohydrate residues of glycoproteins of ASFV oligosaccharides and lectin-like receptors of swine red blood cells.

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

Cited by 59 publications

References 29 publications

Improved Strategy for Molecular Characterization of African Swine Fever Viruses from Sardinia, Based on Analysis of p30, CD2V and I73R /I329L Variable Regions

Improved Strategy for Molecular Characterization of African Swine Fever Viruses from Sardinia, Based on Analysis of p30, CD2V and I73R /I329L Variable Regions

A Proteomic Atlas of the African Swine Fever Virus Particle

THE HAEMADSORPTION AT AFRICAN SWINE FEVER (review)

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