Authors:

Edwin Legall

Date Created:

Not specified

Course Title:

Professor:

Not specified

About Paper:

Human Enterovirus D68 (EV-D68) is a respiratory virus that infects young children, causing a range of mild to severe respiratory illness and has been implicated in Acute Flaccid Myelitis (AFM), a neurologic condition that causes polio-like paralysis. Mature EV-D68 capsids are comprised of 60 units called protomers, each of which contain 3 external structural proteins, VP1-VP3, and an internal structural protein, VP4. VP4 is dynamic and highly conserved across enterovirus species and has been found to be critical in all stages of the viral life cycle. Current studies on VP4 highlight its role in the EV-D68 life cycle, necessary modifications that are required for infection, and its necessity for viral breathing. However, analysis of specific residues that contribute to particle stability and successful infection remains unclear. In this study, VP4 residue phenylalanine 32 (F32) was mutated to introduce amino acid substitutions in VP4 to ala, trp, and tyr (VP4 F32A, F32W, and F32Y respectively). We hypothesize that mutations within this conserved residue will disrupt interactions within the capsid and will decrease capsid stability and therefore impair host cell entry. Further analysis will be done by performing plaque assays, viral growth curves, thermostability assays, and entry assays. Results will be compared to WT EV-D68 to evaluate the significance of this residue on particle stability and virus entry. Understanding the importance of this residue can provide valuable insight about capsid dynamics and potentially lead to the development of a pan-enterovirus vaccine or anti-viral therapeutic.

Source:

Purdue University / 2023

Topics:

No topics listed

Co-authors:

Edwin Legall