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Updated: Apr 15, 2026

An In Vitro Model for Studying Cellular Transformation by Kaposi Sarcoma Herpesvirus
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Glycosylation of KSHV encoded vGPCR functions in its signaling and tumorigenicity

Hui Wu1, Liqun Liu2, Jun Xiao3

  • 1Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education of China, College of Life Science, Hunan Normal University, Changsha 410081, China. wu2hui218@sina.com.cn.

Viruses
|April 4, 2015
PubMed

Insights

N-linked glycosylation of the KSHV vGPCR is essential for its cell surface transport and oncogenic activity. Ablating glycosylation impairs signaling and tumor formation, highlighting glycosylation

Area of Science:

  • Oncology
  • Virology
  • Molecular Biology

Background:

  • Kaposi's sarcoma-associated herpesvirus (KSHV) is a tumor virus responsible for Kaposi's Sarcoma (KS).
  • The KSHV G protein-coupled receptor (vGPCR) is an oncogene linked to KSHV-associated malignancies.

Purpose of the Study:

  • To investigate the role of N-linked glycosylation in vGPCR function and tumorigenesis.
  • To determine the specific sites of glycosylation on vGPCR and their impact on its biological activity.

Main Methods:

  • Site-directed mutagenesis to ablate N-linked glycosylation sites on vGPCR.
  • Immunofluorescence assays to assess vGPCR trafficking to the cellular membrane.
  • Cellular signaling assays and xenograph nude mouse models to evaluate vGPCR's oncogenic potential.

Main Results:

  • vGPCR undergoes extensive N-linked glycosylation at specific asparagine residues (18, 22, 31, and 202).
  • N-linked glycosylation is crucial for vGPCR trafficking to the plasma membrane.
  • vGPCR mutants lacking glycosylation sites failed to activate downstream signaling and were impaired in inducing tumor formation.

Conclusions:

  • Glycosylation is critical for vGPCR-mediated tumorigenesis.
  • Proper vGPCR function and signaling depend on its presence at the plasma membrane, regulated by glycosylation.

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