How the Universal MSA52 Aptamer Recognizes the SARS-CoV‑2 Spike Protein.

ABSTRACT: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the pathogen responsible for the COVID-19 pandemic. The prominent characteristic of SARS-CoV-2 is the use of a trimeric spike (S) glycoprotein to invade the host cell; therefore, the S protein has become a major drug and vaccine target. Recently, a universal aptamer (MSA52) has been reported to bind to the S protein of seven former variants of concern (VOCs) in both glycan and nonglycan forms. However, no molecular details regarding these interactions are currently available. Thus, in this work, molecular dynamics (MD) simulations were performed to understand the binding of MSA52 to the S protein in both its nonglycosylated (NG) and glycosylated (G) forms. In the NG, MSA52 is inserted between the receptor binding domain (RBD)

SUBMITTER: Awang T 

PROVIDER: S-EPMC12509022 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature