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Nature Communications· 2026Q1

A divergent betacoronavirus with a functional furin cleavage site in South American bats

K. Takada, Nicholas Yamahoki, Jonathon C. O. Mifsud, Itsuki Anzai et al.

Short summary

A novel bat betacoronavirus from Brazil, distinct enough to warrant a new subgenus, possesses a functional furin cleavage site (RDAR motif) in its spike protein, a feature previously linked to increased virulence in human coronaviruses.

AI-generated from the title and abstract; the full text is not read.

Key points

  • A novel betacoronavirus was identified in Pteronius parnellii bats in Brazil.
  • Phylogenetic analysis suggests the virus represents a new betacoronavirus subgenus.
  • The virus's spike protein features a functional furin cleavage site with an RDAR motif.
  • This RDAR motif differs by one amino acid from the RRAR motif in SARS-CoV-2.
  • Furin cleavage sites appear to be a structurally permissive 'hotspot' for incorporation in bat coronaviruses.

AI-generated from the title and abstract; the full text is not read.

Abstract

Abstract Bats are natural reservoirs for a wide range of RNA viruses. Members of the genus Betacoronavirus , including Severe Acute Respiratory Syndrome virus 2 (SARS-CoV-2) and Middle East Respiratory Syndrome virus (MERS-CoV), have attracted particular attention due to their recent zoonotic emergence. However, much of the known diversity of betacoronaviruses is based on data from Asia, Africa, and the Middle East, with limited genomic information available from the Americas. Herein, we report the complete genome of a novel bat betacoronavirus identified from a Pteronotus parnellii bat sampled in Brazil. Phylogenetic analysis revealed that this virus is sufficiently distinct from the five recognized Betacoronavirus subgenera to represent a new subgenus. Of note, the spike protein of this novel bat coronavirus possesses a functional furin cleavage site at the S1/S2 junction with a unique amino acid sequence motif (RDAR) that differs from that found in SARS-CoV-2 (RRAR) by only one amino acid. Comparative structural analysis identified other betacoronaviruses in bats with furin cleavage sites at the S1/S2 junction, suggesting that this region is a structurally permissive “hotspot” for cleavage site incorporation. Our study provides a broader understanding of the phylogenetic and functional diversity of bat coronaviruses as well as their zoonotic potential.

The authors' abstract, as published at the source. Nature Communications, 2026 · DOI ↗

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Field: Animal Science and Zoology

Animal Science and ZoologyAgricultural and Biological Sciences