The carbohydrate binding protein Scytovirin acts as an antiviral entry inhibitor.  Structural engineering has been used to improve Scytovirin's ability to protect against the HIV-1 infection.  15N-HSQC spectra for Scytovirin and eleven mutant forms were analyzed.  The changes in chemical shift caused by mutating one amino acid were mapped onto the structure.  Resonances were assigned by inspection and categorized by the magnitude of the chemical shift change.  It was determined that mutations in various regions were more likely to affect the protein core than others.  Overall, Scytovirin is structurally resistant to amino acid changes, opening the possibility of structural engineering to reduce cost and increase efficacy.

Visualizing the effects of mutations in Scytovirin

245th National Meeting (2013)

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