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- W2092156350 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." @default.
- W2092156350 created "2016-06-24" @default.
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- W2092156350 date "2015-01-01" @default.
- W2092156350 modified "2023-10-07" @default.
- W2092156350 title "Structural properties of a viral orthologue of cellular CD200 protein: KSHV vOX2" @default.
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- W2092156350 doi "https://doi.org/10.1016/j.virol.2014.10.020" @default.
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