Nipah virus entry can occur by macropinocytosis

Journal Article · Sun Dec 20 04:00:00 EST 2009 · Virology

DOI:https://doi.org/10.1016/j.virol.2009.09.016· OSTI ID:21357577

Pernet, Olivier; Pohl, Christine; Ainouze, Michelle; Kweder, Hasan ^[1]; Buckland, Robin ^[1]

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1. Molecular Basis of Paramyxovirus Entry, INSERM U758 Virologie Humaine IFR 128 BioSciences Gerland-Lyon Sud, 21 Avenue Tony Garnier, 69365 Lyon Cedex 07 (France)

Nipah virus (NiV) is a zoonotic biosafety level 4 paramyxovirus that emerged recently in Asia with high mortality in man. NiV is a member, with Hendra virus (HeV), of the Henipavirus genus in the Paramyxoviridae family. Although NiV entry, like that of other paramyxoviruses, is believed to occur via pH-independent fusion with the host cell's plasma membrane we present evidence that entry can occur by an endocytic pathway. The NiV receptor ephrinB2 has receptor kinase activity and we find that ephrinB2's cytoplasmic domain is required for entry but is dispensable for post-entry viral spread. The mutation of a single tyrosine residue (Y304F) in ephrinB2's cytoplasmic tail abrogates NiV entry. Moreover, our results show that NiV entry is inhibited by constructions and drugs specific for the endocytic pathway of macropinocytosis. Our findings could potentially permit the rapid development of novel low-cost antiviral treatments not only for NiV but also HeV.

• OSTI ID: 21357577
• Journal Information: Virology, Journal Name: Virology Journal Issue: 2 Vol. 395; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
AMINO ACIDS
CARBOXYLIC ACIDS
HYDROXY ACIDS
MEMBRANE PROTEINS
MICROORGANISMS
MUTATIONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PROTEINS
RECEPTORS
RESIDUES
TYROSINE
VIRUSES