ABSTRACTVIRAL GLYCOPROTEINS AND ENDOPLASMIC RETICULUM-ASSOCIATEDDEGRADATIONByDylan Alexander-Aldo FrabuttEnveloped viruses are responsible for many virulent diseases of critical concern topublic health. As a prerequisite for infectivity, enveloped viruses must mount viralproteins into host membranes in order to facilitate binding and entry into their targetcell population. These membrane proteins are often heavily glycosylated and aresubject to the unique folding environment in the endoplasmic reticulum, which consistsof the host machinery necessary for maintaining the protein homeostasis either throughfolding assistance or degradation of proteins unable to fold properly. I haveinvestigated both of these aforementioned roles through the characterization of HIV-1and influenza A virus envelope interactions with the endoplasmic reticulum chaperonescalnexin and calreticulin and the roles that class I α 1,2-mannosidases play in thedegradation of these viral envelope glycoproteins. Additionally my work has sought tocharacterize how different viruses activate the unfolded response when producing theirenvelope glycoproteins and how this activation may influence viral infections.
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