Proteins specified by African swine fever virus

Tabarés, E.; Marcotegui, M. A.; Fernández, M.; Sanchez-Botija, C.

doi:10.1007/bf01314979

Cited by 59 publications

(9 citation statements)

References 18 publications

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“…This number is consistent with the 151 "major" ORFs present in the viral genome, taking into account the limitations of the 2-DE technique. As expected, this number is larger than the 42 induced polypeptides found using 1-D gels [15]. The molecular mass value of the ASFV-induced polypeptides ranged from 220 kDa to 7.9 kDa.…”

Section: Discussionsupporting

confidence: 64%

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African swine fever virus-induced polypeptides in porcine alveolar macrophages and in Vero cells: Two-dimensional gel analysis

2001

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High-resolution two-dimensional electrophoresis followed by computer analysis has been used to study quantitatively the patterns of protein synthesis produced in porcine alveolar macrophages and in Vero cells infected with African swine fever virus (ASFV). Initially, a protein database for each cell type was constructed. The porcine alveolar macrophage database includes 995 polypeptides (818 acidic, isoelectric focusing (IEF) and 177 basic, nonequilibrium pH gradient electrophoresis (NEPHGE)) whereas the Vero database contains 1,398 polypeptides (1,127 acidic, IEF and 271 basic, NEPHGE). Taking these databases as reference, ASFV highly virulent strain E70 induces 57 acid and 43 basic polypeptides in porcine alveolar macrophages, which account for most of the information content of the virus DNA. The kinetics of synthesis of the virus-induced polypeptides showed the existence of three classes of proteins: one whose synthesis starts early after infection, continues for a period and then switches off; another whose synthesis also starts early but continues for prolonged periods; and a third which requires DNA replication. The attenuated, cell adapted, strain BA71V induces 92 acidic and 37 basic proteins in Vero cells. Significant differences were observed when comparing the patterns of polypeptides induced by the two viral strains. In both cell systems studied, ASFV infection produces a general shutoff of protein synthesis that affects up to 65% of the cellular proteins. Interestingly, 28 proteins of porcine alveolar macrophages and 48 proteins of Vero cells are stimulated at least two times by ASFV infection.

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Section: Discussionsupporting

confidence: 64%

“…About 35 polypeptides have been reported to be induced in ASFV infected cells as analyzed by 1-D polyacrylamide electrophoresis [15], a number that increased to 95 when 2-DE was applied [16]. Surprisingly, until now, there has not been a detailed study of ASFV induced polypeptides in the natural target cell, the porcine macrophage.…”

Section: Introductionmentioning

confidence: 99%

African swine fever virus-induced polypeptides in porcine alveolar macrophages and in Vero cells: Two-dimensional gel analysis

2001

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“…This could indicate that the sera correspond to animals in late stages of infection. The protein p12, the major ASFV-induced protein in infected cells, 13 seems to be the first protein to induce antibodies in infected pigs.…”

Section: Confirmation Of Asfv-elisa-positive Field Pig Sera By Ripa Amentioning

confidence: 99%

Comparison of a Radioimmunoprecipitation Assay to Immunoblotting and ELISA for Detection of Antibody to African Swine Fever Virus

et al. 1990

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A radioimmunoprecipitation assay (RIPA) has been developed for detection of antibody to African swine fever virus (ASFV) and compared with the immunoblot assay with regard to sensitivity and specificity. Two hundred seven field sera, obtained from pigs in Spain from different geographic areas between 1975 and 1986, that were positive by ASFV enzyme-linked immunosorbent assay (ELISA) were also analysed by immunoblot assay and RIPA. By serum dilution experiments, the RIPA appeared at least as sensitive as the ELISA and immunoblotting tests, although ELISA and RIPA detected antibodies to ASFV earlier in natural infection than did the immunoblot assay, as disclosed by animal inoculation studies. The most antigenic ASFV-induced proteins in natural infection detected by RIPA were the viral proteins p243, p172, p73, p25.5, p15, and p12 and the infection proteins p30 and p23.5. In the immunoblot assay, the proteins that were most reactive with the same sera were the viral protein p25.5 and the infection proteins p30, p25, and p21.5. Only 1 serum, from an animal infected with ASFV, was negative by immunoblot assay but showed a positive result by RIPA. A modification of conventional RIPA was performed using a dot transference of immunoprecipitated proteins to a nitrocellulose filter. This modification simplified the conventional RIPA procedures by eliminating the electrophoresis of immunoprecipitated proteins without affecting sensitivity and specificity. The ease of use, specificity, and the sensitivity comparable to that of the immunoblot assay make the RIPA a useful confirmatory assay for sera that yield conflicting results in other ASFV antibody assays.

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“…Expression of viral proteins during the infection cycle is regulated in a temporal fashion, and proteins are classified as early or late on the basis of their requirement for viral DNA synthesis (48,53). Some virus proteins undergo posttranslational modifications such as glycosylation (21,52), phosphorylation (45,52), proteolytic processing (37), or fatty acid acylation (2).…”

mentioning

confidence: 99%

Sequence and characterization of the major early phosphoprotein p32 of African swine fever virus

Prados¹,

Viñuela²,

Alcamı́³

1993

J Virol

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The gene encoding protein p32, the most abundant and immunogenic protein induced by African swine fever virus at early times of infection, has been mapped in the EcoRI C' fragment of the genome of the Vero cell-adapted virus strain BA71V. Sequencing analysis has shown the existence of an open reading frame, named C'204L, encoding 204 amino acids. The protein is phosphorylated in serine residues located in the 115 N-terminal amino acids and was phosphorylated when expressed in cells infected with a vaccinia virus recombinant. Protein p32 is not glycosylated in spite of the presence of two putative N-glycosylation sites in the deduced amino acid sequence of the polypeptide. Immunofluorescence experiments have shown that the protein is localized in the cytoplasm of infected cells and not in the plasma membrane. In addition, the protein has been found in the soluble fraction and not in microsomes from BA71V-infected Vero cells. Low levels of the protein have been detected in the medium from infected swine macrophages, which probably corresponds to nonspecific release of cytoplasmic proteins. The protein encoded by other virus isolates shows different electrophoretic mobilities, indicating variability of p32.

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Proteins specified by African swine fever virus

Cited by 59 publications

References 18 publications

African swine fever virus-induced polypeptides in porcine alveolar macrophages and in Vero cells: Two-dimensional gel analysis

African swine fever virus-induced polypeptides in porcine alveolar macrophages and in Vero cells: Two-dimensional gel analysis

Comparison of a Radioimmunoprecipitation Assay to Immunoblotting and ELISA for Detection of Antibody to African Swine Fever Virus

Sequence and characterization of the major early phosphoprotein p32 of African swine fever virus

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