Henipavirus mediated membrane fusion, virus entry and targeted therapeutics Journal Article


Authors: Steffen, D. L.; Xu, K.; Nikolov, D. B.; Broder, C. C.
Article Title: Henipavirus mediated membrane fusion, virus entry and targeted therapeutics
Abstract: The Paramyxoviridae genus Henipavirus is presently represented by the type species Hendra and Nipah viruses which are both recently emerged zoonotic viral pathogens responsible for repeated outbreaks associated with high morbidity and mortality in Australia, Southeast Asia, India and Bangladesh. These enveloped viruses bind and enter host target cells through the coordinated activities of their attachment (G) and class I fusion (F) envelope glycoproteins. The henipavirus G glycoprotein interacts with host cellular B class ephrins, triggering conformational alterations in G that lead to the activation of the F glycoprotein, which facilitates the membrane fusion process. Using the recently published structures of HeV-G and NiV-G and other paramyxovirus glycoproteins, we review the features of the henipavirus envelope glycoproteins that appear essential for mediating the viral fusion process, including receptor binding, G-F interaction, F activation, with an emphasis on G and the mutations that disrupt viral infectivity. Finally, recent candidate therapeutics for henipavirus-mediated disease are summarized in light of their ability to inhibit HeV and NiV entry by targeting their G and F glycoproteins. © 2012 by the authors; licensee MDPI, Basel, Switzerland.
Keywords: unclassified drug; review; nonhuman; mutant protein; binding affinity; protein conformation; protein function; protein localization; protein protein interaction; inhibitor; immunotherapy; models, molecular; antivirus agent; receptor; drug therapy; antibody; glycoprotein; ribavirin; oligomerization; receptor binding; virus attachment; chloroquine; antiviral agents; viral fusion proteins; thrombospondin; virus entry; virus mutation; ephrin b2; virus infectivity; host-pathogen interactions; virus cell interaction; membrane fusion; virus neutralization; ephrin b3; henipavirus; nipah virus; paramyxovirus; ephrin-b3; viral envelope proteins; paramyxoviridae; virus internalization; virus envelope protein; ephrin-b2; entry; attachment glycoprotein; fusion glycoprotein; glycoprotein f; monoclonal antibody m102 4; henipavirus infection; nipah virus infection; virus envelope; henipavirus infections
Journal Title: Viruses
Volume: 4
Issue: 2
ISSN: 1999-4915
Publisher: MDPI  
Date Published: 2012-02-01
Start Page: 280
End Page: 309
Language: English
DOI: 10.3390/v4020280
PROVIDER: scopus
PMCID: PMC3315217
PUBMED: 22470837
DOI/URL:
Notes: --- - "Export Date: 2 April 2012" - "Source: Scopus"
Altmetric
Citation Impact
MSK Authors
  1. Dimitar B Nikolov
    73 Nikolov
  2. Kai Xu
    20 Xu