The SARS-CoV-2 Omicron variant acquired high infectivity through more than 30 mutations in its spike protein, but the detailed molecular mechanism remained unclear. The research group of Hisashi Arase (RIMD/ IFReC/ CiDER/ CAMaD, The University of Osaka) revealed that mutations in the Omicron spike protein increased the number of positively charged amino acid residues, thereby enhancing its affinity for negatively charged heparan sulfate on the cell surface. They suggest that this enhanced affinity enables efficient infection of cells with low ACE2 receptor expression.
(online publishing in mBio on June 23, 2025 EST)

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Prof. Hisashi Arase

arasebiken.osaka-u.ac.jp

Immunochemistry