HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Ghildyal, R. Articles by Mills, J. Search for Related Content PubMed PubMed Citation Articles by Ghildyal, R. Articles by Mills, J. Agricola Articles by Ghildyal, R. Articles by Mills, J.

Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein

Michael N. Teng^5,

¹ Department of Respiratory and Sleep Medicine, Monash Medical Centre, 246 Clayton Road, Clayton 3168, Australia
² Departments of Microbiology and Medicine, Monash University, Clayton, Australia
³ Department of Environmental Biology, RMIT University, Melbourne, Australia
⁴ Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia
⁵ Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, MA, USA

Correspondence
Reena Ghildyal
reena.ghildyal{at}med.monash.edu.au

Paramyxovirus assembly at the cell membrane requires the movement of viral components to budding sites and envelopment of nucleocapsids by cellular membranes containing viral glycoproteins, facilitated by interactions with the matrix protein. The specific protein interactions during assembly of respiratory syncytial virus (RSV) are unknown. Here, the postulated interaction between the RSV matrix protein (M) and G glycoprotein (G) was investigated. Partial co-localization of M with G was demonstrated, but not with a truncated variant lacking the cytoplasmic domain and one-third of the transmembrane domain, in cells infected with recombinant RSV or transfected to express G and M. A series of G mutants was constructed with progressively truncated or modified cytoplasmic domains. Data from co-expression in cells and a cell-free binding assay showed that the N-terminal aa 2–6 of G play a key role in G–M interaction, with serine at position 2 and aspartate at position 6 playing key roles.

Present address: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, PA, USA.

This article has been cited by other articles:

				M. Batonick, A. G. P. Oomens, and G. W. Wertz Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells J. Virol., September 1, 2008; 82(17): 8664 - 8672. [Abstract] [Full Text] [PDF]

				D. Li, D. A. Jans, P. G. Bardin, J. Meanger, J. Mills, and R. Ghildyal Association of Respiratory Syncytial Virus M Protein with Viral Nucleocapsids Is Mediated by the M2-1 Protein J. Virol., September 1, 2008; 82(17): 8863 - 8870. [Abstract] [Full Text] [PDF]

				M. Tahara, M. Takeda, and Y. Yanagi Altered Interaction of the Matrix Protein with the Cytoplasmic Tail of Hemagglutinin Modulates Measles Virus Growth by Affecting Virus Assembly and Cell-Cell Fusion J. Virol., July 1, 2007; 81(13): 6827 - 6836. [Abstract] [Full Text] [PDF]

				H. D. Pantua, L. W. McGinnes, M. E. Peeples, and T. G. Morrison Requirements for the Assembly and Release of Newcastle Disease Virus-Like Particles J. Virol., November 15, 2006; 80(22): 11062 - 11073. [Abstract] [Full Text] [PDF]

				A. G. P. Oomens, K. P. Bevis, and G. W. Wertz The Cytoplasmic Tail of the Human Respiratory Syncytial Virus F Protein Plays Critical Roles in Cellular Localization of the F Protein and Infectious Progeny Production J. Virol., November 1, 2006; 80(21): 10465 - 10477. [Abstract] [Full Text] [PDF]