Previous Article | Next Article ![]()
J. Virol., Jan 1995, 172-181, Vol 69, No. 1
AR Stewart, AE Tollefson, P Krajcsi, SP Yei and WS Wold
The adenovirus type 2 and 5 E3 10,400- and 14,500-molecular-weight (10.4K
and 14.5K) proteins are both required to protect some cell lines from lysis
by tumor necrosis factor and to down-regulate the epidermal growth factor
receptor. We have shown previously that both 10.4K and 14.5K are integral
membrane proteins and that 14.5K is phosphorylated and O glycosylated. The
10.4K protein coimmunoprecipitates with 14.5K, indicating that the two
proteins function as a complex. Here we show, using immunofluorescence and
two different cell surface-labeling techniques, that both proteins are
localized in the plasma membrane. In addition, we show that trafficking of
each protein to the plasma membrane depends on concomitant expression of
the other protein. Finally, neither protein could be immunoprecipitated
from conditioned media, indicating that neither is secreted. Taken
together, these results suggest that the plasma membrane is the site at
which 10.4K and 14.5K function to inhibit cytolysis by tumor necrosis
factor and to down-regulate the epidermal growth factor receptor.
Copyright © 1995, American Society for Microbiology
The adenovirus E3 10.4K and 14.5K proteins, which function to prevent cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor, are localized in the plasma membrane
Department of Molecular Microbiology and Immunology, St. Louis University School of Medicine, Missouri 63104.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|