<i>C</i>₃-Symmetric Aromatic Core of Griffithsin Is Essential for Potent Anti-HIV Activity.

ABSTRACT: Lectins, carbohydrate-binding proteins of nonimmune origin, bind to carbohydrates and glycan shields present on the surfaces of cells and viral spike proteins. Lectins thus hold great promise as therapeutic and diagnostic proteins, exemplified by their potent antiviral activities and the desire to engineer synthetic carbohydrate receptors based on lectin recognition principles. Here, we describe a new carbohydrate-binding architectural motif─namely, a C₃-symmetric tyrosine-based aromatic core, present in the therapeutic lectin griffithsin (GRFT). By using structure-based amino acid substitutions, X-ray crystallography, molecular dynamics (MD) simulations, and HIV-1 neutralization assays, we show that this core is critical for potent (pM) antiviral activity and nanomolar b

SUBMITTER: Sun J 

PROVIDER: S-EPMC10091857 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature