4C7L

Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase

Summary for 4C7L

• Entry DOI: 10.2210/pdb4c7l/pdb
• Related: 4C7W
• Descriptor: HEMAGGLUTININ-ESTERASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: hydrolase, receptor destroying, receptor binding, 4-o-acetylated sialic acid
• Biological source: MURINE HEPATITIS VIRUS
• Total number of polymer chains: 2
• Total formula weight: 93450.82

Authors

Zeng, Q.H.,Huizinga, E.G. (deposition date: 2013-09-23, release date: 2013-10-09, Last modification date: 2023-12-20)

Primary citation

Langereis, M.A.,Zeng, Q.,Heesters, B.A.,Huizinga, E.G.,De Groot, R.J.
The Murine Coronavirus Hemagglutinin-Esterase Receptor-Binding Site: A Major Shift in Ligand Specificity Through Modest Changes in Architecture.
Plos Pathog., 8:02492-, 2012

PubMed Abstract: The hemagglutinin-esterases (HEs), envelope glycoproteins of corona-, toro- and orthomyxoviruses, mediate reversible virion attachment to O-acetylated sialic acids (O-Ac-Sias). They do so through concerted action of distinct receptor-binding ("lectin") and receptor-destroying sialate O-acetylesterase ("esterase") domains. Most HEs target 9-O-acetylated Sias. In one lineage of murine coronaviruses, however, HE esterase substrate and lectin ligand specificity changed dramatically as these viruses evolved to use 4-O-acetylated Sias instead. Here we present the crystal structure of the lectin domain of mouse hepatitis virus (MHV) strain S HE, resolved both in its native state and in complex with a receptor analogue. The data show that the shift from 9-O- to 4-O-Ac-Sia receptor usage primarily entailed a change in ligand binding topology and, surprisingly, only modest changes in receptor-binding site architecture. Our findings illustrate the ease with which viruses can change receptor-binding specificity with potential consequences for host-, organ and/or cell tropism, and for pathogenesis.

PubMed: 22291594
DOI: 10.1371/JOURNAL.PPAT.1002492

Experimental method

X-RAY DIFFRACTION (2.1 Å)