INHIBITION OF CELLULAR PROTEIN SECRETION BY POLIOVIRUS PROTEINS 2B AND 3A
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作者:
DOEDENS, JR
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UNIV COLORADO, HOWARD HUGHES MED INST, DEPT MOLEC CELLULAR & DEV BIOL, BOULDER, CO 80309 USAUNIV COLORADO, HOWARD HUGHES MED INST, DEPT MOLEC CELLULAR & DEV BIOL, BOULDER, CO 80309 USA
DOEDENS, JR
[1
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KIRKEGAARD, K
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UNIV COLORADO, HOWARD HUGHES MED INST, DEPT MOLEC CELLULAR & DEV BIOL, BOULDER, CO 80309 USAUNIV COLORADO, HOWARD HUGHES MED INST, DEPT MOLEC CELLULAR & DEV BIOL, BOULDER, CO 80309 USA
KIRKEGAARD, K
[1
]
机构:
[1] UNIV COLORADO, HOWARD HUGHES MED INST, DEPT MOLEC CELLULAR & DEV BIOL, BOULDER, CO 80309 USA
Poliovirus RNA replication occurs on the surface of membranous vesicles that proliferate throughout the cytoplasm of the infected cell. Since at least some of these vesicles are thought to originate within the secretory pathway of the host cell, we examined the effect of poliovirus infection on protein transport through the secretory pathway. We found that transport of both plasma membrane and secretory proteins was inhibited by poliovirus infection early in the infectious cycle. Transport inhibition did not require viral RNA replication or the inhibition of host cell translation by poliovirus. The viral proteins 2B and 3A were each sufficient to inhibit transport in the absence of viral infection. The intracellular localization of a secreted protein in the presence of 3A with the endoplasmic reticulum suggested that 3A directly blocks transport from the endoplasmic reticulum to the Golgi apparatus.