Structural Basis for Ligand and Substrate Recognition by Torovirus Hemagglutinin Esterases
Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases Martijn A. Langereisa,1, Qinghong Zengb,1, Gerrit J. Gerwigc, Barbara Freyd, Mark von Itzsteind, Johannis P. Kamerlingc, Raoul J. de Groota,2,3, and Eric G. Huizingab,2,3 aVirology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, bCrystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Faculty of Sciences, and cDepartment of Bio-Organic Chemistry, Bijvoet Center for Biomolecular Research, Faculty of Sciences, Utrecht University, 3584 CH Utrecht, The Netherlands; and dInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia Edited by Peter Palese, Mount Sinai School of Medicine, New York, NY, and approved July 14, 2009 (received for review April 24, 2009) Hemagglutinin esterases (HEs), closely related envelope glycopro- to subunit 1 of the influenza C virus hemagglutinin–esterase teins in influenza C and corona- and toroviruses, mediate reversible fusion (HEF) protein. While toro- and coronaviruses are of attachment to O-acetylated sialic acids (Sias). They do so by acting common ancestry, they apparently acquired their HE genes both as lectins and as receptor-destroying enzymes, functions exerted through horizontal gene transfer on separate occasions after the by separate protein domains. HE divergence was accompanied by torovirus–coronavirus split (3). Structural and bioinformatic changes in quaternary structure and in receptor and substrate spec- evidence suggests that the nidovirus HEs originated from trim- ificity. The selective forces underlying HE diversity and the molecular eric HEF-like fusion proteins (7–9). In the course of events, the basis for Sia specificity are poorly understood.
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