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Cover Picture: The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin‐Neuraminidase Revealed (Angew. Chem. Int. Ed. 10/2015)
Author(s) -
Dirr Larissa,
ElDeeb Ibrahim M.,
Guillon Patrice,
Carroux Cindy J.,
Chavas Leonard M. G.,
von Itzstein Mark
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201500511
Subject(s) - sialic acid , stereochemistry , covalent bond , chemistry , neuraminidase , biology , virus , virology , biochemistry , organic chemistry
The human parainfluenza virus type 3 (hPIV‐3) is one of the leading causes of lower respiratory tract disease in children. In their Communication on page 2936 ff., M. von Itzstein, I. M. El‐Deeb, P. Guillon, L. M. G. Chavas, and co‐workers investigate the catalytic mechanism of hPIV‐3 haemagglutinin‐neuraminidase (HN) and determine that it is a retaining glycohydrolase. Moreover hPIV‐3 HN utilizes a highly conserved tyrosine residue to form a transient covalent bond with the anomeric carbon of the substrate. Finally a novel sialic acid derivative showed potency in virus blockade assays.