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© The Rockefeller University Press, 0021-9525/1999//945 $5.00
The Journal of Cell Biology, Volume 147, Number 5, , 1999 945-958

Original Article

Replication of Tobacco Mosaic Virus on Endoplasmic Reticulum and Role of the Cytoskeleton and Virus Movement Protein in Intracellular Distribution of Viral RNA



Paloma Mása and Roger N. Beachya

a Division of Plant Biology, Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037
Donald Danforth Plant Science Center, 7425 Forsyth Blvd., Box 1098, Clayton, MO 63130.(314) 935-8605(314) 935-9852

rnbeachy{at}danforthcenter.org

Little is known about the mechanisms of intracellular targeting of viral nucleic acids within infected cells. We used in situ hybridization to visualize the distribution of tobacco mosaic virus (TMV) viral RNA (vRNA) in infected tobacco protoplasts. Immunostaining of the ER lumenal binding protein (BiP) concurrent with in situ hybridization revealed that vRNA colocalized with the ER, including perinuclear ER. At midstages of infection, vRNA accumulated in large irregular bodies associated with cytoplasmic filaments while at late stages, vRNA was dispersed throughout the cytoplasm and was associated with hair-like protrusions from the plasma membrane containing ER. TMV movement protein (MP) and replicase colocalized with vRNA, suggesting that viral replication and translation occur in the same subcellular sites. Immunostaining with tubulin provided evidence of colocalization of vRNA with microtubules, while disruption of the cytoskeleton with pharmacological agents produced severe changes in vRNA localization. Mutants of TMV lacking functional MP accumulated vRNA, but the distribution of vRNA was different from that observed in wild-type infection. MP was not required for association of vRNA with perinuclear ER, but was required for the formation of the large irregular bodies and association of vRNA with the hair-like protrusions.

Key Words: in situ hybridization • tobacco mosaic virus • virus replication • endoplasmic reticulum • cytoskeleton

© 1999 The Rockefeller University Press

BFA, Brefeldin ABiP, lumenal binding proteinCP, coat proteinfluor-RNA, fluorescein-RNAGFP, green fluorescent proteinhpi, hours post-infectionMP, movement proteinTMV, tobacco mosaic viruswt, wild-type

Roger N. Beachy's current address is Donald Danforth Plant Science Center, Clayton, MO 63130.


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