INVESTIGADORES
REY Osvaldo
artículos
Título:
The E7 oncoprotein of human papillomavirus type 16 interacts with F-actin in vitro and in vivo.
Autor/es:
REY O, LEE S, BALUDA MA, SWEE J, ACKERSON B, CHIU R, PARK NH.
Revista:
VIROLOGY
Editorial:
ACADEMIC PRESS INC ELSEVIER SCIENCE
Referencias:
Año: 2000 p. 372 - 381
ISSN:
0042-6822
Resumen:
We report here that E7 oncoprotein of human papillomavirus type 16
(HPV-16) forms a complex in vivo and in vitro with actin, one of the
components of the cellular cytoskeleton. The in vivo interaction was
detected by immunofluorescent staining and confocal microscopic
examination of normal human oral keratinocytes (NHOK) and CV-1 cells
after transient expression of E7 employing the vaccinia virus-T7 RNA
polymerase system and by coimmunoprecipitation from an immortalized,
nontumorigenic cell line obtained after transfecting NHOK with the
cloned HPV-16 DNA genome. The in vitro interaction was detected by
cosedimentation of bacterially expressed E7 phosphorylated with rabbit
reticulocyte lysate or purified casein kinase II (CKII) prior to
incubation with F-actin. This interaction was inhibited if E7
phosphorylation by the rabbit reticulocyte lysate was prevented with
heparin, a CKII inhibitor, or if the amino acids Ser-31 and Ser-32 in
E7, which are phosphorylated by CKII, were replaced with amino acids
that cannot be phosphorylated. Interestingly, a decrease in the amount
of polymerized actin occurred in cells expressing E7.