Title: "Why Does HCMV Encode A Glycoprotein H Complex That Lacks Glycoprotein L?"
Speaker: Jeremy Kamil, PhD / LSU Health, Shreveport
Host: Richard Longnecker, PhD
Topic:
In many enveloped viruses, a single glycoprotein suffices to bind host receptors and fuse membranes to initiate infection. Herpesviruses, however, encode a large number of glycoproteins, several of which play roles in immune evasion and never leave the endoplasmic reticulum, while other glycoproteins, comprised of or built upon glycoprotein H (gH)/ glycoprotein L (gL) heterodimers, bind receptors to regulate membrane fusion events which are catalyzed by glycoprotein B, the proximal fusogen for all herpesviruses. Human cytomegalovirus (HCMV), the so called “prototype” betaherpesvirus, encodes at least three glycoprotein H complexes, one of which, gH/UL116, lacks the canonical gH dimerization partner, gL. I will share results that suggest a function for this complex.
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Dr. Richard Longnecker
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