Heat-shock protein 70 is associated with the entry of Marek's disease virus into fibroblast

Related Experiment Video

Updated: May 28, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
07:14

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

Published on: March 8, 2024

Xiao-Jia Wang1

  • 1China Agricultural University, Beijing, People's Republic of China. wangxj@cau.edu.cn

Acta Virologica
|October 8, 2011
PubMed

Insights

Heat shock protein 70 (HSP70) acts as a cellular receptor for Marek's disease virus (MDV) glycoprotein gH. This interaction is crucial for early-stage MDV entry into chicken cells, advancing our understanding of viral infection.

Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • Interactions between Marek's disease virus (MDV) entry glycoproteins and cellular receptors are not well understood.
  • Limited literature exists on the specific receptors involved in MDV entry.

Purpose of the Study:

  • To identify the cellular receptor for the MDV glycoprotein gH.
  • To elucidate the role of this receptor in the early stages of MDV infection.

Main Methods:

  • Western blot analysis to identify potential cellular receptors.
  • Co-immunoprecipitation assays to confirm protein interactions.
  • Plaque inhibition assays to assess viral entry into chicken embryo fibroblasts (CEF).

Main Results:

  • Heat shock protein 70 (HSP70) was identified as a potential cellular receptor binding to MDV glycoprotein gH.
  • HSP70 was confirmed to be involved in the early stages of MDV entry into CEF.
  • This binding interaction facilitates the MDV infection process.

Conclusions:

  • HSP70 plays a significant role as a cellular receptor in MDV entry by interacting with gH.
  • This finding enhances the understanding of both HSP70's functions and the MDV infection mechanism.

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