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A time‐related study of Brefeldin A effects in HSV‐1 infected cultured human fibroblasts
Author(s) -
JENSEN HELLE LONE,
RYGAARD JØRGEN,
NORRILD BODIL
Publication year - 1995
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1995.tb01402.x
Subject(s) - brefeldin a , herpes simplex virus , golgi apparatus , intracellular , tubulin , virus , immunofluorescence , colchicine , organoid , chemistry , microbiology and biotechnology , in vitro , glycoprotein , confocal microscopy , microtubule , biology , biophysics , endoplasmic reticulum , virology , biochemistry , antibody , immunology , genetics
Glycoprotein D (gD‐1) is an essential virion envelope component of herpes simplex virus type 1 (HSV‐1) normally transported to the plasma membrane of the infected cells. In the present study, the intracellular transport of gD‐1 was inhibited in cultured HSV‐1 infected human fibroblasts by Brefeldin A (BFA) 1μg/ml medium added for 12 h after virus adsorption. Immunofluorescence light‐ and confocal microscopy revealed abolished transport of gD‐1 to the plasma membrane, juxtanuclear accumulation of gD‐1, and a disorderly arrangement of the tubulin fibres. Withdrawal of BFA influence for more than 60 min resulted in incomplete transport but increasing accumulation of gD‐1 in the plasma membrane and in Golgi‐like areas close to the nuclei. The tubulin pattern was almost normalized 6 h after removal of BFA. The egress of infectious HSV‐1 particles released 9 h post‐BFA treatment was not fully reestablished. The results indicate that BFA effects were not completely reversible and caused a sort of cytotoxic influence involving the structure of tubulin.