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Vol. 13, Issue 8, 2795-2809, August 2002
and
*Institute of Biochemistry, Hannover Medical School, Hannover
D-30623, Germany; and After fusion of the viral envelope with the plasma membrane, herpes
simplex virus type 1 (HSV1) capsids are transported along microtubules
(MTs) from the cell periphery to the nucleus. The motor ATPase
cytoplasmic dynein and its multisubunit cofactor dynactin mediate most
transport processes directed toward the minus-ends of MTs.
Immunofluorescence microscopy experiments demonstrated that HSV1
capsids colocalized with cytoplasmic dynein and dynactin. We blocked
the function of dynein by overexpressing the dynactin subunit
dynamitin, which leads to the disruption of the dynactin complex. We
then infected such cells with HSV1 and measured the efficiency of
particle binding, virus entry, capsid transport to the nucleus, and the
expression of immediate-early viral genes. High concentrations of
dynamitin and dynamitin-GFP reduced the number of viral capsids
transported to the nucleus. Moreover, viral protein synthesis was
inhibited, whereas virus binding to the plasma membrane, its
internalization, and the organization of the MT network were not
affected. We concluded that incoming HSV1 capsids are propelled along
MTs by dynein and that dynein and dynactin are required for efficient
viral capsid transport to the nucleus.
Department of Pathology, Columbia
University, New York, NY 10032-3702
Corresponding author. E-mail address:
Sodeik.Beate{at}MH-Hannover.de.
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