Published in Cell Reports, Pfaff-Kilgore and colleagues describe a comprehensive mutagenesis and functional study (545 individual mutants) of the E1E2 protein of Hepatitis C that enabled us to develop a model of how each amino acid is used in the function of this virus.
Thank you to our scientific team at Integral Molecular and collaborators in the laboratories of Drs. Nicasio Mancini, Justin Bailey, James Crowe, and Mansun Law who made this study possible.
Highlights
- Test 545 hepatitis C virus (HCV) E1E2 envelope mutations for infectivity and antibody binding
- Identify residues important for HCV E1E2 folding, interaction and infectivity
- HCV E1E2 is a fragile protein complex where most mutations compromise function
- Functional residues of E1E2 are highly conserved across genotypes
