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Journal of Virology, November 1999, p. 9664-9668, Vol. 73, No. 11
Department of Pharmacology and Toxicology and
Biocenter Oulu,1 Department of Internal
Medicine,5 and Department of
Anatomy,2 University of Oulu, 90220 Oulu,
Finland; Department of Internal Medicine, University of
Iowa College of Medicine, and The Veterans Affairs Medical Center,
Iowa City, Iowa4; and Division of
Immunologic and Infectious Diseases, The Children's Hospital of
Philadelphia, Philadelphia, Pennsylvania 191043
Received 3 May 1999/Accepted 9 August 1999
Adenovirus interaction with
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
rab5 GTPase Regulates Adenovirus
Endocytosis
v integrins is important for virus
entry. We have examined the effects of adenovirus attachment on
intracellular signaling in HeLa cells, with an emphasis on pathways
known to be activated following integrin interaction with other
ligands. We found no evidence for
[Ca2+]c-mediated signaling or for tyrosine
phosphorylation of pp125FAK, p130CAS, and
paxillin. However, adenovirus attachment is known to activate phosphatidylinositol-3 kinase, which in turn may regulate endocytosis via rab5 GTPase. We found that adenovirus uptake was increased by
overexpression of wild-type rab5 and decreased by dominant-negative rab5. These results indicate a role for rab5 in adenovirus entry.
*
Corresponding author. Mailing address: University of
Oulu, Department of Pharmacology and Toxicology, Kajaanintie 52D, 90220 Oulu, Finland. Phone: (358)-(0)8-537 5240. Fax: (358)-(0)8-537 5247. E-mail: thautala{at}sun3.oulu.fi.
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