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

doi:10.1016/j.virol.2014.10.020

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

Medical Sciences

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	94-104
Number of pages	11
Journal	Virology
Volume	474
DOIs	https://doi.org/10.1016/j.virol.2014.10.020
Publication status	Published - 1 Jan 2015

Bibliographical note

Funding Information:
The authors acknowledge the helpful contribution of Dr. Christine Milburn (University of St Andrews) for her work in performing PNGase digestions. This work was funded by grants to D.J.B. from the Medical Research Council (MRC; G0400408 and G0800154 ), BBSRC ( BBS/B/14442 ), and CR UK ( C7934 ). The authors acknowledge the support of the Vice Chancellor of Research, Mashhad University of Medical Sciences , Mashhad, Iran (Grant no: MUMS 900118 ).

Publisher Copyright:
© 2014.

Keywords

CD200
Glycosylation
Homology modelling
KSHV
RGD domain
VOX2

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10.1016/j.virol.2014.10.020

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title = "Structural properties of a viral orthologue of cellular CD200 protein: KSHV vOX2",

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.",

keywords = "CD200, Glycosylation, Homology modelling, KSHV, RGD domain, VOX2",

author = "{Ali Amini}, Abbas and Solovyova, {Alexandra S.} and Hamid Sadeghian and Blackbourn, {David J.} and Rezaee, {S. A.Rahim}",

note = "Funding Information: The authors acknowledge the helpful contribution of Dr. Christine Milburn (University of St Andrews) for her work in performing PNGase digestions. This work was funded by grants to D.J.B. from the Medical Research Council (MRC; G0400408 and G0800154 ), BBSRC ( BBS/B/14442 ), and CR UK ( C7934 ). The authors acknowledge the support of the Vice Chancellor of Research, Mashhad University of Medical Sciences , Mashhad, Iran (Grant no: MUMS 900118 ). Publisher Copyright: {\textcopyright} 2014.",

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doi = "10.1016/j.virol.2014.10.020",

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AU - Ali Amini, Abbas

AU - Solovyova, Alexandra S.

AU - Sadeghian, Hamid

AU - Blackbourn, David J.

AU - Rezaee, S. A.Rahim

N1 - Funding Information: The authors acknowledge the helpful contribution of Dr. Christine Milburn (University of St Andrews) for her work in performing PNGase digestions. This work was funded by grants to D.J.B. from the Medical Research Council (MRC; G0400408 and G0800154 ), BBSRC ( BBS/B/14442 ), and CR UK ( C7934 ). The authors acknowledge the support of the Vice Chancellor of Research, Mashhad University of Medical Sciences , Mashhad, Iran (Grant no: MUMS 900118 ). Publisher Copyright: © 2014.

PY - 2015/1/1

Y1 - 2015/1/1

N2 - 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.

AB - 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.

KW - CD200

KW - Glycosylation

KW - Homology modelling

KW - KSHV

KW - RGD domain

KW - VOX2

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SP - 94

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JO - Virology

JF - Virology

ER -

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

Abstract

Bibliographical note

Keywords

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