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

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 i...

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Published inMedChemComm Vol. 8; no. 1; pp. 130 - 134
Main Authors El-Deeb, Ibrahim M., Guillon, Patrice, Dirr, Larissa, von Itzstein, Mark
Format Journal Article
LanguageEnglish
Published CAMBRIDGE Royal Soc Chemistry 01.01.2017
Subjects
Biochemistry & Molecular Biology
Chemistry, Medicinal
Life Sciences & Biomedicine
Paramyxoviridae
Pharmacology & Pharmacy
Science & Technology
TARGET
INFECTIONS
POTENT
CHILDHOOD RESPIRATORY-DISEASE
EFFICACY
ANALOGS
BCX 2798
MICE
DISCOVERY
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Summary: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.
Bibliography:Australian Research Council
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ISSN:2040-2503
2040-2511
DOI:10.1039/c6md00519e