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

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.

• Authors: Ibrahim M El-Deeb, Patrice Guillon, Larissa Dirr, Mark von Itzstein
• Journal: MedChemComm (Medchemcomm) Vol. 8 Issue 1 Pg. 130-134 (Jan 01 2017) ISSN: 2040-2503 [Print] England
• PMID: 30108698 (Publication Type: Journal Article)