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*
Institute for Virus Research and
Department of Geriatric Medicine, Graduate School of Medicine, Kyoto University, Kyoto, Japan; and
Department of Bioscience, National Cardiovascular Center Research Institute, Suita, Japan
Adhesion of bacteria to vascular endothelial cells as well as
mucosal cells and epithelial cells appears to be one of the initial
steps in the process of bacterial infection, including infective
endocarditis. We examined whether lectin-like oxidized low-density
lipoprotein receptor 1 (LOX-1), a member of scavenger receptor family
molecules with C-type lectin-like structure, can support adhesion of
Gram-positive and Gram-negative bacteria. Chinese hamster ovary-K1
(CHO-K1) cells stably expressing LOX-1 can support binding of
FITC-labeled Staphylococcus aureus and
Escherichia coli, which was suppressed by poly(I) and an
anti-LOX-1 mAb. Adhesion of these bacteria to LOX-1 does not
require divalent cations or serum factors and can be supported under
both static and nonstatic conditions. Cultured bovine aortic
endothelial cells (BAEC) can also support adhesion of FITC-labeled
S. aureus, which was similarly suppressed by poly(I) and
an anti-LOX-1 mAb. In contrast, binding of FITC-labeled E.
coli to BAEC was partially inhibited by the anti-LOX-1 mAb,
and poly(I) did not block FITC-labeled E. coli adhesion
to BAEC, but, rather, enhanced it under a static condition. TNF-
increased LOX-1-dependent adhesion of E. coli, but not
that of S. aureus, suggesting that S.
aureus adhesion to BAEC may require additional molecules, which
cooperate with LOX-1 and suppressed by TNF-
. Taken together, LOX-1
can work as a cell surface receptor for Gram-positive and Gram-negative
bacteria, such as S. aureus and E. coli,
in a mechanism similar to that of class A scavenger receptors; however,
other unknown molecules may also be involved in the adhesion of
E. coli to BAEC, which is enhanced by
poly(I).
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