What question did this study set out to answer?

The study aims to understand how SARS-CoV-2 and bat coronaviruses recognize their receptors, particularly ACE2.

February 13, 2026Open Access

Structural basis for bat receptor recognition by SARS-CoV-2 and bat SARS2-like coronaviruses

Key Points

The study aims to understand how SARS-CoV-2 and bat coronaviruses recognize their receptors, particularly ACE2.
Comparison of receptor-binding domains (RBDs) of SARS-CoV-2 and BANAL-52
Structural and biochemical analyses of interactions with human and bat ACE2
Examination of specific amino acid interactions related to binding affinity
BANAL-52 RBD binds well to bat ACE2 due to favorable amino acid interactions
SARS-CoV-2 RBD shows stronger binding to human ACE2 due to specific residues
Findings reveal evolutionary insights regarding receptor adaptation in coronaviruses

Abstract

Coronaviruses evolve to optimize receptor recognition in their natural hosts. A key mystery of COVID-19 is why the SARS-CoV-2 receptor-binding domain (RBD) binds human ACE2 with such high affinity despite limited time for adaptation, while some bat-derived RBDs paradoxically bind human ACE2 more strongly than bat ACE2. To investigate, we compared the RBDs of SARS-CoV-2 and BANAL-52, a related bat coronavirus, examining their interactions with ACE2 from Rhinolophus sinicus (RsBat) and from human. Structural and biochemical analyses revealed that BANAL-52 RBD is well adapted for binding to RsBat ACE2, with His498 of BANAL-52 RBD pairing favorably with His41 of RsBat ACE2. By contrast, SARS-CoV-2 RBD favors human ACE2, largely due to His34 and Met82 in human ACE2, residues that generally enhance RBD binding. These results show that receptor recognition by SARS-CoV-2 and related bat coronaviruses is consistent with established structural principles and provide structural insights relevant to the evolutionary origins of COVID-19.

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