Abstract
T cells interact with the extracellular matrix via integrin receptors and these interactions affect both cellular localization and proliferation. The importance of these interactions in retrovirus-induced diseases, however, remains less clear. In the present study, we investigated changes in T cell adhesion to extracellular matrix proteins by HTLV-I expressing cell lines and human peripheral blood lymphocytes infected with HTLV-I by cocultivation. Cell lines and acutely infected primary peripheral blood lymphocytes demonstrated enhanced adhesion to fibronectin. Acute infection of peripheral blood lymphocytes increased the expression of α5β1 and α4β1 integrins. Antibodies to the α4,α5, and β1 subunits inhibited attachment of infected cells to fibronectin. We conclude that HTLV-I infection is associated with an increase in the expression of both the classical fibronectin receptor and the receptor for the alternatively spliced domain of fibronectin on peripheral blood lymphocytes. HTLV-I-related alterations in cell surface adhesion molecules may contribute to the abnormal proliferation of T cells in adult T cell leukemia (ATL) or to the abnormal localization of activated or infected T cells to the central nervous system of patients with tropical spastic paraparesis/HTLV-I-associated myelopathy (TSP/HAM).