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Journal of Virology, November 2002, p. 11186-11198, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11186-11198.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Membrane Fusion Tropism and Heterotypic Functional Activities of the Nipah Virus and Hendra Virus Envelope Glycoproteins

Katharine N. Bossart,1 Lin-Fa Wang,2 Michael N. Flora,3 Kaw Bing Chua,4 Sai Kit Lam,5 Bryan T. Eaton,2 and Christopher C. Broder1*

Department of Microbiology and Immunology,1 Biomedical Instrumentation Center, Uniformed Services University, Bethesda, Maryland 20814,3 CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Victoria 3220, Australia,2 International Medical University, Sesama Centre, Bukit Jalil, 57000 Kuala Lumpur,4 Department of Medical Microbiology, University of Malaya Medical Center, 50603 Kuala Lumpur, Malaysia5

Received 3 May 2002/ Accepted 1 August 2002

Nipah virus (NiV) and Hendra virus (HeV) are novel paramyxoviruses from pigs and horses, respectively, that are responsible for fatal zoonotic infections of humans. The unique genetic and biological characteristics of these emerging agents has led to their classification as the prototypic members of a new genus within the Paramyxovirinae subfamily called Henipavirus. These viruses are most closely related to members of the genus Morbillivirus and infect cells through a pH-independent membrane fusion event mediated by the actions of their attachment (G) and fusion (F) glycoproteins. Understanding their cell biological features and exploring the functional characteristics of the NiV and HeV glycoproteins will help define important properties of these emerging viruses and may provide new insights into paramyxovirus membrane fusion mechanisms. Using a recombinant vaccinia virus system and a quantitative assay for fusion, we demonstrate NiV glycoprotein function and the same pattern of cellular tropism recently reported for HeV-mediated fusion, suggesting that NiV likely uses the same cellular receptor for infection. Fusion specificity was verified by inhibition with a specific antiserum or peptides derived from the {alpha}-helical heptads of NiV or HeV F. Like that of HeV, NiV-mediated fusion also requires both F and G. Finally, interactions between the glycoproteins of the paramyxoviruses have not been well defined, but here we show that the NiV and HeV glycoproteins are capable of highly efficient heterotypic functional activity with each other. However, no heterotypic activity was observed with envelope glycoproteins of the morbilliviruses Measles virus and Canine distemper virus.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, F. Edward Hébert School of Medicine, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Rd., Bethesda, MD 20814-4799. Phone: (301) 295-3401. Fax: (301) 295-1545. E-mail: cbroder{at}usuhs.mil.

Journal of Virology, November 2002, p. 11186-11198, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11186-11198.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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