Remodeling the Endoplasmic Reticulum by Poliovirus Infection and by Individual Viral Proteins: an Autophagy-Like Origin for Virus-Induced Vesicles

Journal of Virology - Tập 74 Số 19 - Trang 8953-8965 - 2000
David Suhy1, Thomas H. Giddings2, Karla Kirkegaard1
1Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305,1 and
2Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado 803092

Tóm tắt

ABSTRACT All positive-strand RNA viruses of eukaryotes studied assemble RNA replication complexes on the surfaces of cytoplasmic membranes. Infection of mammalian cells with poliovirus and other picornaviruses results in the accumulation of dramatically rearranged and vesiculated membranes. Poliovirus-induced membranes did not cofractionate with endoplasmic reticulum (ER), lysosomes, mitochondria, or the majority of Golgi-derived or endosomal membranes in buoyant density gradients, although changes in ionic strength affected ER and virus-induced vesicles, but not other cellular organelles, similarly. When expressed in isolation, two viral proteins of the poliovirus RNA replication complex, 3A and 2C, cofractionated with ER membranes. However, in cells that expressed 2BC, a proteolytic precursor of the 2B and 2C proteins, membranes identical in buoyant density to those observed during poliovirus infection were formed. When coexpressed with 2BC, viral protein 3A was quantitatively incorporated into these fractions, and the membranes formed were ultrastructurally similar to those in poliovirus-infected cells. These data argue that poliovirus-induced vesicles derive from the ER by the action of viral proteins 2BC and 3A by a mechanism that excludes resident host proteins. The double-membraned morphology, cytosolic content, and apparent ER origin of poliovirus-induced membranes are all consistent with an autophagic origin for these membranes.

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Tài liệu tham khảo

10.1006/bbrc.1995.1010

10.1128/JVI.72.11.8988-9001.1998

10.1128/IAI.66.3.950-958.1998

10.1083/jcb.139.7.1687

10.1016/0042-6822(87)90063-8

10.1128/jvi.66.5.2740-2747.1992

10.1128/jvi.64.3.1156-1163.1990

10.1128/jvi.11.4.565-574.1973

10.1128/JVI.74.14.6556-6563.2000

10.1006/viro.1994.1329

10.1002/jemt.1060130305

10.1016/0042-6822(65)90001-2

10.1128/jvi.71.12.9054-9064.1997

10.1002/j.1460-2075.1995.tb07071.x

Dubois-Dalcq M. Holmes K. V. Rentier B. Assembly of enveloped RNA viruses. 1984 Springer-Verlag Vienna Austria

10.1083/jcb.110.6.1923

10.1083/jcb.110.6.1935

10.1128/jvi.70.12.8675-8683.1996

10.1083/jcb.107.6.2075

10.1089/hyb.1995.14.347

10.1099/0022-1317-6-1-151

10.1128/jvi.71.12.9490-9498.1997

10.1128/jvi.69.8.5142-5146.1995

10.1016/0042-6822(92)90178-R

10.1016/S0021-9258(17)42314-3

10.1128/JVI.72.11.8586-8596.1998

10.1038/45257

10.1083/jcb.136.1.61

10.1006/viro.1997.8906

10.1128/jvi.66.4.1985-1994.1992

10.1006/viro.1994.1110

10.1093/oxfordjournals.jbchem.a022225

10.1038/30529

10.1128/JVI.73.3.2016-2026.1999

10.1006/viro.1995.1192

10.1084/jem.136.5.1117

10.1007/BF00492453

10.1016/S0021-9258(18)53068-4

10.1128/jvi.71.6.4679-4693.1997

10.1016/0003-2697(87)90587-2

10.1128/jvi.70.10.6576-6588.1996

10.1242/jcs.108.6.2477

Sheeler P. Density gradient centrifugation Centrifugation in biology and medical science. Sheeler P. 1981 81 99 John Wiley & Sons Inc. New York N.Y

10.1083/jcb.121.3.521

10.1042/bj3350217

10.1074/jbc.274.14.9183

10.1128/iai.63.9.3609-3620.1995

10.1128/jvi.71.12.8962-8972.1997

10.1074/jbc.271.43.26810

10.1146/annurev.cb.06.110190.003435

10.1074/jbc.274.21.15222

10.1128/JVI.73.9.7641-7657.1999

10.1083/jcb.118.5.1015

Watzele G. Bachofner R. Berger E. G. Immunocytochemical localization of the Golgi apparatus using protein-specific antibodies to galactosyltransferase.Eur. J. Cell Biol. 56 1991 451 458

10.1016/0003-2697(84)90782-6

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Journal of Virology

Tập 74 Số 19

8953-8965

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