This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pantua, H. Articles by Morrison, T. G. Search for Related Content PubMed PubMed Citation Articles by Pantua, H. Articles by Morrison, T. G.

 Previous Article  |  Next Article 

Journal of Virology, September 2005, p. 11660-11670, Vol. 79, No. 18
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.18.11660-11670.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of an Alternate Form of Newcastle Disease Virus Fusion Protein

Homer Pantua,³ Lori W. McGinnes,¹ John Leszyk,² and Trudy G. Morrison^1,3*

Department of Molecular Genetics and Microbiology,¹ Department of Biochemistry and Molecular Biology,² Program in Immunology/Virology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 01655³

Received 17 December 2004/ Accepted 27 May 2005

The sequence and structure of the Newcastle disease virus (NDV) fusion (F) protein are consistent with its classification as a type 1 glycoprotein. We have previously reported, however, that F protein can be detected in at least two topological forms with respect to membranes in both a cell-free protein synthesizing system containing membranes and infected COS-7 cells (J. Virol. 77:1951-1963, 2003). One form is the classical type 1 glycoprotein, while the other is a polytopic form in which approximately 200 amino acids of the amino-terminal end as well as the cytoplasmic domain (CT) are translocated across membranes. Furthermore, we detected CT sequences on surfaces of F protein-expressing cells, and antibodies specific for these sequences inhibited red blood cell fusion to hemagglutinin-neuraminidase and F protein-expressing cells, suggesting a role for surface-expressed CT sequences in cell-cell fusion. Extending these findings, we have found that the alternate form of the F protein can also be detected in infected and transfected avian cells, the natural host cells of NDV. Furthermore, the alternate form of the F protein was also found in virions released from both infected COS-7 cells and avian cells by Western analysis. Mass spectrometry confirmed its presence in virions released from avian cells. Two different polyclonal antibodies raised against sequences of the CT domain of the F protein slowed plaque formation in both avian and COS-7 cells. Antibody specific for the CT domain also inhibited single-cycle infections, as detected by immunofluorescence of viral proteins in infected cells. The potential roles of this alternate form of the NDV F protein in infection are discussed.

---

* Corresponding author. Mailing address: University of Massachusetts Medical School, Dept. of MGM, Rm. S5-250, 55 Lake Avenue North, Worcester, MA 01655. Phone: (508) 856-6592. Fax: (508) 856-5920. E-mail: trudy.morrison{at}umassmed.edu.

---

Journal of Virology, September 2005, p. 11660-11670, Vol. 79, No. 18
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.18.11660-11670.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Jain, S., McGinnes, L. W., Morrison, T. G. (2009). Role of Thiol/Disulfide Exchange in Newcastle Disease Virus Entry. J. Virol. 83: 241-249 [Abstract] [Full Text]  
• Laliberte, J. P., McGinnes, L. W., Morrison, T. G. (2007). Incorporation of Functional HN-F Glycoprotein-Containing Complexes into Newcastle Disease Virus Is Dependent on Cholesterol and Membrane Lipid Raft Integrity. J. Virol. 81: 10636-10648 [Abstract] [Full Text]