The Murid Herpesvirus-4 gH/gL Binds to Glycosaminoglycans
2008
Murid Herpesvirus-4 gH/gL Binds to Glycosaminoglycans
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Gillet Laurent, Colaco Susanna, Stevenson Philip G.
Primary Institution: University of Cambridge
Hypothesis
How do the glycoproteins gp70, gp150, and gH/gL interact with glycosaminoglycans during Murid Herpesvirus-4 infection?
Conclusion
Murid Herpesvirus-4 relies on multiple glycoproteins to bind to glycosaminoglycans for effective cell entry.
Supporting Evidence
- Murid Herpesvirus-4 is highly dependent on glycosaminoglycans for cell binding.
- Deleting gp150 frees MuHV-4 from GAG dependence.
- GAG binding by gH/gL explains redundancy with gp70.
Takeaway
The virus uses special proteins to stick to cells, which helps it get inside and cause infection.
Methodology
The study involved expressing recombinant gH/gL and testing its binding to cells, along with various antibody blocking experiments.
Limitations
The study does not provide direct evidence for the interaction between gB and gp150.
Statistical Information
P-Value
p<0.00001
Statistical Significance
p<0.00001
Digital Object Identifier (DOI)
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