Recent Emergence of Bovine Coronavirus Variants with Mutations in the Hemagglutinin-Esterase Receptor Binding Domain in U.S. Cattle

Authors

Aspen M. Workman, USDA, Agricultural Research ServiceFollow
Tara G. McDaneld, USDA, Agricultural Research Service
Gregory P. Harhay, USDA, Agricultural Research ServiceFollow
Subha Das, South Dakota State University
John Dustin Loy, University of Nebraska-Lincoln
Benjamin M. Hause, South Dakota State University

Document Type

Article

Date of this Version

9-27-2022

Citation

Workman, A.M.; McDaneld, T.G.; Harhay, G.P.; Das, S.; Loy, J.D.; Hause, B.M. Recent Emergence of Bovine Coronavirus Variants with Mutations in the Hemagglutinin-Esterase Receptor Binding Domain in U.S. Cattle. Viruses 2022, 14, 2125. https:// doi.org/10.3390/v14102125

Comments

Open access.

Abstract

Bovine coronavirus (BCoV) has spilled over to many species, including humans, where the host range variant coronavirus OC43 is endemic. The balance of the opposing activities of the surface spike (S) and hemagglutinin-esterase (HE) glycoproteins controls BCoV avidity, which is critical for interspecies transmission and host adaptation. Here, 78 genomes were sequenced directly from clinical samples collected between 2013 and 2022 from cattle in 12 states, primarily in the Midwestern U.S. Relatively little genetic diversity was observed, with genomes having >98% nucleotide identity. Eleven isolates collected between 2020 and 2022 from four states (Nebraska, Colorado, California, and Wisconsin) contained a 12 nucleotide insertion in the receptor-binding domain (RBD) of the HE gene similar to one recently reported in China, and a single genome from Nebraska collected in 2020 contained a novel 12 nucleotide deletion in the HE gene RBD. Isogenic HE proteins containing either the insertion or deletion in the HE RBD maintained esterase activity and could bind bovine submaxillary mucin, a substrate enriched in the receptor 9-O-acetylated-sialic acid, despite modeling that predicted structural changes in the HE R3 loop critical for receptor binding. The emergence of BCoV with structural variants in the RBD raises the possibility of further interspecies transmission.