TY - JOUR
T1 - Vesicular stomatitis virus and sindbis virus glycoprotein transport to the cell surface is inhibited by ionophores
AU - Johnson, David C.
AU - Schlesinger, Milton J.
N1 - Funding Information:
We are indebted to T. Rucinsky and G. Phillips for their excellent technical assistance in electron microscopic examinations. E. Elson and R. Gibson are thanked for helpful discussions. This work w’as supported by DHEW Grant 2ROl CA 14311. The Washington University Center for Basic Cancer Research (funded by DHEW Grant 5P30 CA 16217) provided tissue culture media and material for electron microscopy.
PY - 1980/6
Y1 - 1980/6
N2 - The effect of two cationic ionophores, monensin and A23187, on the replication of Sindbis and vesicular stomatitis virus in cultures of BHK and chicken embryo fibroblast cells has been studied. Treating these cells with the ionophores at 10-6, M 2 hr prior to infection at high multiplicities of infection did not affect viral protein synthesis but severely inhibited release of viral particles into the media. Glycoproteins of these viruses were synthesized in normal amounts but they did not appear on the surface of infected cells. Proteolytic cleavage of Sindbis virus glycoprotein PE2 to E2 was inhibited in ionophore-treated cells, although fatty acid attachment to PE2 proceeded normally. Fatty acid attachment to VSV G protein and the posttranslational removal of mannose residues from G oligosaccharides occurred in the drug-treated cells. These data indicate that these ionophores block the movement of viral glycoproteins from the Golgi apparatus to the cell surface membrane where budding and release of these two viruses occur.
AB - The effect of two cationic ionophores, monensin and A23187, on the replication of Sindbis and vesicular stomatitis virus in cultures of BHK and chicken embryo fibroblast cells has been studied. Treating these cells with the ionophores at 10-6, M 2 hr prior to infection at high multiplicities of infection did not affect viral protein synthesis but severely inhibited release of viral particles into the media. Glycoproteins of these viruses were synthesized in normal amounts but they did not appear on the surface of infected cells. Proteolytic cleavage of Sindbis virus glycoprotein PE2 to E2 was inhibited in ionophore-treated cells, although fatty acid attachment to PE2 proceeded normally. Fatty acid attachment to VSV G protein and the posttranslational removal of mannose residues from G oligosaccharides occurred in the drug-treated cells. These data indicate that these ionophores block the movement of viral glycoproteins from the Golgi apparatus to the cell surface membrane where budding and release of these two viruses occur.
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U2 - 10.1016/0042-6822(80)90200-7
DO - 10.1016/0042-6822(80)90200-7
M3 - Article
C2 - 6247822
AN - SCOPUS:0018903944
SN - 0042-6822
VL - 103
SP - 407
EP - 424
JO - Virology
JF - Virology
IS - 2
ER -