Two-dimensional analysis of african swine fever virus proteins and proteins induced in infected cells

Esteves, Aida; Marques, Maria Isabel; Costa, João

doi:10.1016/0042-6822(86)90384-3

Cited by 93 publications

(68 citation statements)

References 23 publications

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“…Alterations in protein trafficking could alter signals delivered by infected macrophages to bystander lymphocytes. Actin filaments and the Golgi are rearranged in ASFVinfected cells (Carvalho et al, 1988;Ferreira, 1996;Esteves et al, 1986;McCrossan et al, 2001) and SH3P7 could be involved in these rearrangements as it is linked to dynamic actin and to Golgi vesicles in other cell types. However, CD2v is non-essential for virus replication and any effects of its interaction with SH3P7 must therefore also not be required.…”

Section: Discussionmentioning

confidence: 99%

The CD2v protein of African swine fever virus interacts with the actin-binding adaptor protein SH3P7

Kay-Jackson

Goatley

Cox

et al. 2004

Journal of General Virology

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The predicted extracellular domain of the CD2v protein of African swine fever virus (ASFV) shares significant similarity to that of the CD2 protein in T cells but has a unique cytoplasmic domain of unknown function. Here we have shown that CD2v is expressed as a glycoprotein of approximately 105 kDa in ASFV-infected cells. In the absence of an extracellular ligand, the majority of CD2v appears to localize to perinuclear membrane compartments. Furthermore, we have shown using the yeast two-hybrid system and by direct binding studies that the cytoplasmic tail of CD2v binds to the cytoplasmic adaptor protein SH3P7 (mAbp1, HIP55), which has been reported to be involved in diverse cellular functions such as vesicle transport and signal transduction. A cDNA clone encoding a variant form of SH3P7 could also be identified and was found to be expressed in a wide range of porcine tissues. Deletion mutagenesis identified proline-rich repeats of sequence PPPKPC in the ASFV CD2v protein to be necessary and sufficient for binding to the SH3 domain of SH3P7. In ASFV-infected cells, CD2v and SH3P7 co-localized in areas surrounding the perinuclear virus factories. These areas also stained with an antibody that recognizes a Golgi network protein, indicating that they contained membranes derived from the Golgi network. Our data provide a first molecular basis for the understanding of the immunomodulatory functions of CD2v in ASFV-infected animals.

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Section: Discussionmentioning

confidence: 99%

The CD2v protein of African swine fever virus interacts with the actin-binding adaptor protein SH3P7

Kay-Jackson

Goatley

Cox

et al. 2004

Journal of General Virology

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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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“…Strukturproteine auf der äußeren Hülle beschrieben (Esteves et al, 1986). Darunter das Protein 12 (p 12), welches in vitro die Anlagerung von Erythrozyten an infizierte…”

Section: (Abbildung 1) Bisher Wurden 54unclassified

3.3 Afrikanische Schweinepest

Mayr¹

2007

Medizinische Mikrobiologie, Infektions- Und Seuchenlehre

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Two-dimensional analysis of african swine fever virus proteins and proteins induced in infected cells

Cited by 93 publications

References 23 publications

The CD2v protein of African swine fever virus interacts with the actin-binding adaptor protein SH3P7

The CD2v protein of African swine fever virus interacts with the actin-binding adaptor protein SH3P7

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

3.3 Afrikanische Schweinepest

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