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

Lookup NU author(s): Dr Alexandra Solovyova

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Abstract

© 2014. 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.

Publication metadata

Author(s): Ali Amini A, Solovyova AS, Sadeghian H, Blackbourn DJ, Rezaee SAR

Publication type: Article

Publication status: Published

Journal: Virology

Year: 2015

Volume: 474

Pages: 94-104

Print publication date: 01/01/2015

Online publication date: 14/11/2014

Acceptance date: 22/10/2014

ISSN (print): 0042-6822

ISSN (electronic): 1096-0341

Publisher: Academic Press Inc.

URL: https://doi.org/10.1016/j.virol.2014.10.020

DOI: 10.1016/j.virol.2014.10.020

PubMed id: 25463607

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