HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Kay-Jackson, P. C. Articles by Dixon, L. K. Search for Related Content PubMed PubMed Citation Articles by Kay-Jackson, P. C. Articles by Dixon, L. K. Agricola Articles by Kay-Jackson, P. C. Articles by Dixon, L. K.

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

P. C. Kay-Jackson^1,

J. E. Miskin^1,

¹ Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Woking, Surrey GU24 0NF, UK
² Gulbenkian Institute of Science, Oeiras, Portugal
³ Department of Biochemistry and Molecular Immunology, University of Bielefeld, D-33615 Bielefeld, Germany

Correspondence
Linda Dixon
linda.dixon{at}bbsrc.ac.uk

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.

Present address: Department of Cellular Biochemistry, Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany.

Present address: Oxford Biomedica, Medawar Centre, Robert Robinson Avenue, The Oxford Science Park, Oxford OX4 4GA, UK.

This article has been cited by other articles:

				L. S. Heikkinen, A. Kazlauskas, K. Melen, R. Wagner, T. Ziegler, I. Julkunen, and K. Saksela Avian and 1918 Spanish Influenza A Virus NS1 Proteins Bind to Crk/CrkL Src Homology 3 Domains to Activate Host Cell Signaling J. Biol. Chem., February 29, 2008; 283(9): 5719 - 5727. [Abstract] [Full Text] [PDF]

				D. A. G. Chapman, V. Tcherepanov, C. Upton, and L. K. Dixon Comparison of the genome sequences of non-pathogenic and pathogenic African swine fever virus isolates J. Gen. Virol., February 1, 2008; 89(2): 397 - 408. [Abstract] [Full Text] [PDF]

				F. S. Boinas, G. H. Hutchings, L. K. Dixon, and P. J. Wilkinson Characterization of pathogenic and non-pathogenic African swine fever virus isolates from Ornithodoros erraticus inhabiting pig premises in Portugal J. Gen. Virol., August 1, 2004; 85(8): 2177 - 2187. [Abstract] [Full Text] [PDF]