Exploring inhibitor structural features required to engage the 216-loop of human parainfluenza virus type-3 hemagglutinin-neuraminidase

Ibrahim M El-Deeb; Patrice Guillon; Larissa Dirr; Mark von Itzstein

doi:10.1039/c6md00519e

Exploring inhibitor structural features required to engage the 216-loop of human parainfluenza virus type-3 hemagglutinin-neuraminidase

Medchemcomm. 2016 Oct 5;8(1):130-134. doi: 10.1039/c6md00519e. eCollection 2017 Jan 1.

Authors

Ibrahim M El-Deeb¹, Patrice Guillon¹, Larissa Dirr¹, Mark von Itzstein¹

Affiliation

¹ Institute for Glycomics , Griffith University , Gold Coast Campus , Queensland 4222 , Australia . Email: m.vonitzstein@griffith.edu.au.

Abstract

Human parainfluenza virus type-3 is a leading cause of acute respiratory infection in infants and children. There is currently neither vaccine nor clinically effective treatment for parainfluenza virus infection. Hemagglutinin-neuraminidase glycoprotein is a key protein in viral infection, and its inhibition has been a target for inhibitor development. In this study, we explore the structural features required for Neu2en derivatives to efficiently lock-open the 216-loop of the human parainfluenza virus type-3 hemagglutinin-neuraminidase protein.