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Infection of polarized MDCK cells with herpes simplex virus 1: two asymmetrically distributed cell receptors interact
A E Sears1, B S McGwire, B Roizman
1Marjorie B. Kovler Viral Oncology Laboratories, University of Chicago, Chicago, IL 60637.
Abstract:
Herpes simplex virus 1 attaches to at least two cell surface receptors. In polarized epithelial (Madin-Darby canine kidney; MDCK) cells one receptor is located in the apical surface and attachment to the cells requires the presence of glycoprotein C in the virus. The second receptor is located in the basal surface and does not require the presence of glycoprotein C. Exposure of MDCK cells at either the apical or basal surface to wild-type virus yields plaques and viral products whereas infection by a glycoprotein C-negative mutant yields identical results only after exposure of MDCK cells to virus at the basal surface. Multiple receptors for viral entry into cells expand the host range of the virus. The observation that glycoprotein C-negative mutants are infectious in many nonpolarized cell lines suggests that cells in culture may express more than one receptor and explains why genes that specify the viral proteins that recognize redundant receptors, like glycoprotein C, are expendable.
Insights
Herpes simplex virus 1 uses multiple cell receptors for entry. Glycoprotein C is essential for binding to apical receptors on polarized cells but not basal receptors or nonpolarized cells.
Area of Science:
- Virology
- Cell Biology
- Immunology
Background:
- Herpes simplex virus 1 (HSV-1) employs multiple cell surface receptors for entry into host cells.
- Understanding these receptors is crucial for comprehending viral tropism and host range.
Purpose of the Study:
- To investigate the role of glycoprotein C (gC) in HSV-1 attachment and entry into polarized epithelial cells.
- To determine the presence and accessibility of alternative viral receptors on different cell surfaces.
Main Methods:
- Utilized Madin-Darby canine kidney (MDCK) cells, a model for polarized epithelial cells.
- Compared the infectivity of wild-type HSV-1 and a glycoprotein C-negative mutant.
- Assessed viral attachment and plaque formation upon exposure to apical and basal surfaces of MDCK cells.
Main Results:
- Wild-type HSV-1 infected MDCK cells via both apical and basal surfaces, requiring gC for apical attachment.
- Glycoprotein C-negative HSV-1 mutants infected MDCK cells only when exposed to the basal surface.
- Nonpolarized cell lines were infected by gC-negative mutants, suggesting the presence of redundant receptors.
Conclusions:
- HSV-1 utilizes at least two distinct cell surface receptors for entry.
- Glycoprotein C is specifically involved in binding to an apical receptor in polarized epithelial cells.
- The existence of multiple receptors, including those independent of gC, contributes to the virus's broad host range and explains the dispensability of gC in certain contexts.