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Department of Immunology, University of Texas M. D. Anderson Cancer Center, and
Center for Extracellular Matrix Biology, Albert B. Alkek Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, TX 77030
The extracellular matrix protein fibronectin (FN) mediates the
adhesion of bacteria as well as T lymphocytes. Mammalian cells express
integrins 
4
1 and
51 as the major FN-binding cell surface
receptors. Bacteria such as Staphylococcus aureus, also
express FN-binding receptors that are important for adherence to host
tissue and initiation of infection. The S. aureus
FN-binding protein, FnbpA, has been previously identified, and
recombinant proteins that correspond to distinct functional regions of
this protein have been made. Three recombinant truncated forms of
FnbpA, rFnbpA(37-881), rFnbpA(37-605), and rFnbpA(620-881), were
examined for effects on in vitro adhesion and coactivation of human T
lymphocytes. These proteins, when coimmobilized with anti-CD3 mAb,
activated T lymphocyte proliferation. The coactivation signal generated
by the rFnbpA proteins required medium containing serum with FN.
Furthermore, the costimulatory signal could be restored in FN-depleted
serum when the rFnbpAs were preloaded with soluble FN. Monoclonal Ab
blocking studies revealed that integrin
51 is the major receptor responsible for
the rFnbpA costimulatory signal. Shear flow cell detachment assays
confirmed that lymphocytes can bind to FN captured by the rFnbpA
proteins. These results suggest that the S. aureus
rFnbpA can interact with integrin 51 via
an FN bridge to mediate adhesion and costimulatory signals to T
lymphocytes.
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