Previous Article | Next Article ![]()
Journal of Virology, September 1999, p. 7210-7217, Vol. 73, No. 9
Departments of
Medicine1 and
Microbiology,2 University of Alabama at
Birmingham, Birmingham, Alabama 35294-2170
Received 1 February 1999/Accepted 8 May 1999
Among all retroviruses, foamy viruses (FVs) are unique in that they
regularly mature at intracytoplasmic membranes. The envelope glycoprotein of FV encodes an endoplasmic reticulum (ER) retrieval signal, the dilysine motif (KKXX), that functions to localize the human
FV (HFV) glycoprotein to the ER. This study analyzed the function of
the dilysine motif in the context of infectious molecular clones of HFV
that encoded mutations in the dilysine motif. Electron microscopy (EM)
demonstrated virion budding both intracytoplasmically and at the plasma
membrane for the wild-type and mutant viruses. Additionally, mutant
viruses retained their infectivity, but viruses lacking the dilysine
signal budded at the plasma membrane to a greater extent than did
wild-type viruses. Interestingly, this relative increase in budding
across the plasma membrane did not increase the overall release of
viral particles into cell culture media as measured by protein levels
in viral pellets or infectious virus titers. We conclude that the
dilysine motif of HFV imposes a partial restriction on the site of
viral maturation but is not necessary for viral infectivity.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
An Endoplasmic Reticulum Retrieval Signal
Partitions Human Foamy Virus Maturation to Intracytoplasmic
Membranes
*
Corresponding author. Mailing address: University of
Alabama at Birmingham, Division of Infectious Diseases, BBRB 220, Birmingham, AL 35294-2170. Phone: (205) 975-5667. Fax: (205) 975-5718. E-mail: paulg{at}uab.edu.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|