Key result
Chimeric glycoprotein D molecules revealed that a region of HSV-1 gD encompassing amino acids 262-285 is required for cell fusion but not for receptor binding.
Population
Target cells expressing nectin-1 and viral glycoproteins (HSV gB, gH, gL)
Comparison
Chimeric gD molecules composed of HSV and PRV… vs PRV gD or HSV gD
Design
Preclinical
Authors
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May guide HSV entry inhibitor design; leaves open human relevance beyond animal models.
The study identifies that a flexible stalk region in HSV glycoprotein D is critical for membrane fusion, independent of receptor binding.
Zago et al. (2004) studied Herpes simplex virus infection (in vitro). Chimeric glycoprotein D (gD) molecules (HSV-1 and PRV) vs. Wild-type HSV-1 gD and PRV gD was evaluated on Cell fusion activity and receptor binding. Chimeric glycoprotein D molecules revealed that a region of HSV-1 gD encompassing amino acids 262-285 is required for cell fusion but not for receptor binding.
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