Structural properties of a viral orthologue of cellular CD200 protein: KSHV vOX2

Abbas Ali Amini, Alexandra S. Solovyova, Hamid Sadeghian, David J. Blackbourn, S. A.Rahim Rezaee*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Kaposi's sarcoma-associated herpesvirus (KSHV) vOX2 is a cell surface glycoprotein expressed during viral lytic replication to suppress host inflammatory reactions. Here we have characterised vOX2 with biochemical, biophysical and bioinformatics tools and as a result propose a 3-dimensional model for vOX2 based on structural and functional homology with the PD-L1 protein. To validate this model, vOX2 was characterised by analytical ultracentrifugation (AUC) and circular dichroism spectroscopy (CD). The results identified the potential glycosylation sites and revealed that vOX2 is predominantly a beta-folded molecule with an RGD adhesion motif exposed on the C-terminal domain. The protein exists in monomer-dimer equilibrium similar to its IgV-type folded homologues, with 30-36% glycosylation and the molecular weight of the extracellular fragment of molecule is 32.0-33.6. kDa, much less than 50. kDa. Thus, the structural similarity to PD-L1 verifies its immunomodulatory potential and the RGD motif suggests an adhesive capacity.

Original languageEnglish
Pages (from-to)94-104
Number of pages11
JournalVirology
Volume474
DOIs
Publication statusPublished - 1 Jan 2015

Keywords

  • CD200
  • Glycosylation
  • Homology modelling
  • KSHV
  • RGD domain
  • VOX2

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