Emerging SARS-CoV-2 sublineage RE.2.2 displays distinct structural features

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The short version

• Gao George Fu's laboratory at the Institute of Microbiology of the Chinese Academy of Sciences (IMCAS), was published in PNAS .
• The researchers found that RE.2.2 has enhanced binding to the human ACE2 receptor, a distinct antibody escape profile and a previously unobserved N-linked glycosylation site at residue N529 of the spike (S) protein.
• The sublineage BA.3.2.2, derived from omicron BA.3, has shown accelerated spread across several regions of the world.

What happened

Using surface plasmon resonance (SPR) and cryo-electron microscopy (cryo-EM), the researchers determined that the receptor-binding domain (RBD) of RE.2.2 displays high affinity for human angiotensin-converting enzyme 2 (hACE2). Structural analyses revealed that a reverse mutation, R493Q, forms an additional hydrogen bond with hACE2 residue K31, serving as a primary determinant of heightened receptor engagement.

Why it matters

The researchers also tested the interaction of RE.2.2 with ACE2 proteins from different animal species.

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