Open AccessInvolvement of host cell tyrosine phosphorylation in the invasion of HEp‐2 cells by Bartonella bacilliformis
Author(s) -
WilliamsBouyer Natalie M,
Hill E.McGinnis
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13432.x
Subject(s) - biology , genistein , staurosporine , microbiology and biotechnology , tyrosine kinase , human umbilical vein endothelial cell , phosphorylation , protein kinase a , umbilical vein , biochemistry , signal transduction , endocrinology , in vitro
We have provided evidence that exposure of human cells to protein kinase inhibitors results in decreased invasion of these cells by Bartonella bacilliformis in a dose‐dependent manner. Preincubation of human laryngeal epithelial cells in the presence of genistein, a tyrosine protein kinase inhibitor, decreased the invasion of these cells by B. bacilliformis significantly. Further, exposure of normal human umbilical vein endothelial cells to staurosporine, a potent inhibitor of protein kinase C and some tyrosine protein kinases, resulted in a considerable reduction in the number of organisms internalized by these cells. Moreover, Bartonella infection of HEp‐2 cells induced tyrosine phosphorylation of several Triton X‐100 soluble proteins with approximate molecular masses of 243, 215 179, 172 (doublet), 160, 145 and 110 kDa that were absent or reduced in the presence of genistein in cells after 1 h of infection. Exposure of HEp‐2 cell monolayers to anti‐α 5 and anti‐β 1 chain integrin monoclonal antibodies resulted in a moderate decrease in the invasion of these cells, suggesting a possible role of α 5 β 1 integrins in the uptake of Bartonella into nucleated cells.