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B Nuclear Binding and Is Inhibited by Adenovirus-Mediated Expression of Inhibitor of B
1
*
Department of Infectious Diseases, Imperial College School of Medicine (Hammersmith Campus), and
Pediatric Infectious Diseases Unit, St. George’s Hospital Medical School, London, United Kingdom; and
Environmental Protection Agency, Chapel Hill, NC 27514
Respiratory syncytial virus (RSV) infection is an important cause
of lower respiratory tract illness, the severity of which may be partly
due to cellular recruitment. RSV infection activates chemokine
secretion from airway epithelial cells by largely unknown mechanisms.
We investigated the regulation of RSV-induced activation of the
chemokine RANTES in the bronchial epithelial cell line BEAS-2B and
primary normal human tracheobronchial epithelial cultures. RANTES
protein and mRNA were detected at 24 h and up until 72 h from
cultures of BEAS-2B infected with replicating virus, but not with
UV-inactivated RSV. RSV infection of BEAS-2B or normal human
tracheobronchial epithelial cells stimulated NF-
B translocation to
the nucleus and binding to the RANTES-specific B-binding sequences
within 2 h, with levels peaking at 24 h. Supershift assays
indicated that binding was due to p50/p65 heterodimers. BEAS-2B cells
were transfected with a replication-deficient adenoviral vector,
expressing a mutated, nondegradable form of IB
. IB
overexpression specifically blocked NF-B translocation and inhibited
mRNA accumulation and secretion of RANTES induced by RSV or TNF-
plus IFN-
. Adenoviral transfection did not interfere with RSV
replication or significantly induce apoptosis. Further, a control
adenovirus, expressing the ß-galactosidase gene, did not alter
cellular functions. Thus, NF-B nuclear translocation is a critical
step in RSV induction of RANTES secretion. Elucidating the mechanisms
of cellular activation by RSV and targeting specific areas may lead to
novel therapeutic approaches in the treatment of RSV.
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