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Cellular receptor structures for pseudorabies virus are blocked by antithrombin III
A Voigt1, D Sawitzky, H Zeichhardt
1Institute for Clinical and Experimental Virology, Free University Berlin, Germany.
Medical Microbiology and Immunology
|August 1, 1995
Summary
Antithrombin III (ATIII) binding to cell surface heparan sulfate inhibits pseudorabies virus (PrV) attachment. Both PrV glycoprotein C and ATIII bind to similar structures on permissive cells, suggesting a shared cellular receptor interaction mechanism.
Area of Science:
- Virology
- Biochemistry
- Cell Biology
Background:
- Pseudorabies virus (PrV), an alphaherpesvirus, utilizes cellular heparan sulfate as a primary attachment receptor.
- Viral attachment is mediated by envelope glycoprotein C (PrV-gC), which exhibits heparin-binding properties.
- Structural similarities exist between PrV-gC and the heparin-binding site of antithrombin III (ATIII).
Purpose of the Study:
- To investigate the effect of ATIII on the interaction between PrV and its cellular receptor.
- To determine if ATIII and PrV bind to the same cellular structures.
Main Methods:
- Assessing ATIII binding to heparan sulfate residues on RK13 cells.
- Evaluating the impact of ATIII binding on radioactively labeled PrV adsorption.
- Utilizing heparinase I enzymatic treatment to identify receptor components.
- Synthesizing and testing peptides derived from ATIII and PrV-gC for heparin interaction in vitro.
Main Results:
- ATIII specifically bound to heparan sulfate on RK13 cells.
- ATIII binding significantly inhibited PrV adsorption to RK13 cells.
- Heparinase I treatment removed both PrV and ATIII receptors.
- Synthetic peptides from both ATIII and PrV-gC demonstrated specific interaction with heparin.
Conclusions:
- PrV and ATIII interact with the same cellular structures, specifically heparan sulfate residues.
- ATIII can interfere with PrV attachment to host cells, indicating a potential shared binding mechanism.