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Herpes simplex virus type 1 glycoprotein H binds to alphavbeta3 integrins
Christopher Parry1, Susanne Bell1, Tony Minson1
1Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.
The Journal of General Virology
|December 18, 2004
Summary
Herpes simplex virus type 1 glycoprotein H (HSV-1 gH) binds to host cells via the alphavbeta3 integrin. This interaction is mediated by an Arg-Gly-Asp (RGD) motif within the gH ectodomain.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Glycoprotein H (gH) is essential for herpes virus entry into host cells.
- gH homologues are present in all herpes viruses.
- gH is a critical virion envelope glycoprotein.
Purpose of the Study:
- To investigate the cell-binding properties of Herpes simplex virus type 1 (HSV-1) glycoprotein H (gH).
- To identify the specific cellular receptors and motifs involved in HSV-1 gH-mediated cell attachment.
Main Methods:
- Generation of a recombinant soluble form of HSV-1 gH fused to the Fc region of IgG (gHFc-gL).
- Expression in mammalian cells and purification using Protein A Sepharose.
- Cell binding assays using Vero cells and Chinese hamster ovary (CHO) cells, with and without human alphavbeta3 integrin expression.
Main Results:
- The gHFc-gL heterodimer specifically bound to Vero cells.
- Mutation of the Arg-Gly-Asp (RGD) motif in gH abolished cell binding.
- CHO cells did not bind gHFc-gL, but CHO cells expressing human alphavbeta3 integrin showed efficient binding.
Conclusions:
- HSV-1 gH utilizes the human alphavbeta3 integrin for cell attachment.
- The RGD motif within the gH ectodomain is crucial for mediating this integrin-dependent binding.
- This study elucidates a key mechanism of HSV-1 entry.