Human
T-cell leukemia virus type I and type II (HTLV-I and HTLV-II, respectively) infect certain sublines of the BJAB human B-cell line. We observed that the WH subline, but not the CC/84 subline, of BJAB cells were infectible by cell-free HTLV-I or HTLV-II and formed syncytia with cells infected by these retroviruses. This suggests that the BJAB-CC/84 cells possibly lack a membrane molecule(s) important for syncytium formation and infectibility. In order to identify this
antigen, we generated polyclonal anti-BJAB-WH
antisera which were adsorbed on BJAB-CC/84 cells. The adsorbed
antisera bound only BJAB-WH and BJAB-CC/79 cells as demonstrated by
complement-dependent cytotoxicity and flow cytometric assays. Furthermore, this adsorbed
antisera bound several human T-cell clones, including SupT-1, as determined by flow cytometric assays. The adsorbed antiserum was monospecific as it immunoprecipitated only one 78- to 80-kDa
protein from lysates of metabolically labeled BJAB-WH, BJAB-CC/79, and SupT-1, but not BJAB-CC/84, cells. The monospecific
antisera detected a
glycoprotein composed of a 64- to 66-kDa core
protein containing
tunicamycin-sensitive N-linked
oligosaccharides. This
membrane glycoprotein appears to be involved in HTLV-I- and HTLV-II-induced fusion and
infection, as the monospecific
antisera were capable of inhibiting both of these processes. The monospecific
antisera diluted 1:50 and 1:90 inhibited 85 to 90% of syncytium formation induced in BJAB-WH, BJAB-CC/79, and SupT-1 cells cultured with HTLV-I- or HTLV-II-infected MT2, MoT, or FLW human T- or B-cell lines. At the same dilution,
antisera inhibited 70 to 80% of
infection of BJAB-WH cells by cell-free HTLV-I or HTLV-II. Thus, these studies indicate a role for a 78- to 80-kDa
glycoprotein in HTLV-I or
HTLV-II infection and syncytium formation.