Previous Article | Next Article ![]()
Journal of Virology, September 2008, p. 8664-8672, Vol. 82, No. 17
0022-538X/08/$08.00+0 doi:10.1128/JVI.00827-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

and
Gail W. Wertz*
Department of Pathology, University of Virginia, Charlottesville, Virginia 22908
Received 17 April 2008/ Accepted 10 June 2008
Human respiratory syncytial virus (HRSV) is released from the apical membrane of polarized epithelial cells. However, little is known about the processes of assembly and release of HRSV and which viral gene products are involved in the directional maturation of the virus. Based on previous studies showing that the fusion (F) glycoprotein contained an intrinsic apical sorting signal and that N- and O-linked glycans can act as apical targeting signals, we investigated whether the glycoproteins of HRSV were involved in its directional targeting and release. We generated recombinant viruses with each of the three glycoprotein genes deleted individually or in groups. Each deleted gene was replaced with a reporter gene to maintain wild-type levels of gene expression. The effects of deleting the glycoprotein genes on apical maturation and on targeting of individual proteins in polarized epithelial cells were examined by using biological, biochemical, and microscopic assays. The results of these studies showed that the HRSV glycoproteins are not required for apical maturation or release of the virus. Further, deletion of one or more of the glycoprotein genes did not affect the intracellular targeting of the remaining viral glycoproteins or the nucleocapsid protein to the apical membrane.
Published ahead of print on 18 June 2008.
Present address: Center for Veterinary Health Sciences, Oklahoma State University, Stillwater, OK 74078.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»