Receptor-binding loops in alphacoronavirus adaptation and evolution - RIIP - Réseau International des Instituts Pasteur Access content directly
Journal Articles Nature Communications Year : 2017

Receptor-binding loops in alphacoronavirus adaptation and evolution


RNA viruses are characterized by a high mutation rate, a buffer against environmental change. Nevertheless, the means by which random mutation improves viral fitness is not well characterized. Here we report the X-ray crystal structure of the receptor-binding domain (RBD) of the human coronavirus, HCoV-229E, in complex with the ectodomain of its receptor, aminopeptidase N (APN). Three extended loops are solely responsible for receptor binding and the evolution of HCoV-229E and its close relatives is accompanied by changing loop-receptor interactions. Phylogenetic analysis shows that the natural HCoV-229E receptor-binding loop variation observed defines six RBD classes whose viruses have successively replaced each other in the human population over the past 50 years. These RBD classes differ in their affinity for APN and their ability to bind an HCoV-229E neutralizing antibody. Together, our results provide a model for alphacoronavirus adaptation and evolution based on the use of extended loops for receptor binding.
Fichier principal
Vignette du fichier
Correa-Garc-a_et_al-2018-Microbial_Biotechnology.pdf (653.35 Ko) Télécharger le fichier
Origin Files produced by the author(s)

Dates and versions

pasteur-01854628 , version 1 (06-08-2018)




Alan Wong, Aidan Tomlinson, Dongxia Zhou, Malathy Satkunarajah, Kevin Chen, et al.. Receptor-binding loops in alphacoronavirus adaptation and evolution. Nature Communications, 2017, 8 (1), pp.1735. ⟨10.1038/s41467-017-01706-x⟩. ⟨pasteur-01854628⟩


52 View
134 Download



Gmail Mastodon Facebook X LinkedIn More