Generation and characterization of monoclonal antibodies against multiple epitopes on the C-terminal half of envelope gp46 of human T-cell leukemia virus type-I (HTLV-I)

✍ Scribed by Yuetsu Tanaka; Masazumi Yasumoto; Hiroshi Nyunoya; Tsutomu Ogura; Masayoshi Kikuchi; Kunitada Shimotohno; Hiroshi Shiraki; Naotaka Kuroda; Hisatoshi Shida; Hideki Tozawa

• Publisher: John Wiley and Sons
• Year: 1990
• Tongue: French
• Weight: 1000 KB
• Volume: 46
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910460421

✦ Synopsis

In order to study the antigenicity of envelope 46 kDa glycoprotein (gp46) of human T-cell leukemia virus type-I (HTLV-I), we have generated monoclonal anti-gp46 antibodies (MAbs), REY-7, REY-I I, REY-16, REY-30, MET4 and MET-3 from rats and mice. lmmunoblot and immunofluorexence assays showed that these MAbs recognize gp46 and its related antigens, and specifically stained HTLV-I-bearing cells. All MAbs reacted with a recombinant gp46 antigen, N147, expressing the 147 amino acids in the C-terminal half of gp46. By using various synthetic peptides corresponding to the gp46 sequence, epitopes recognized by REY-7 and MET-3, REY-I I and REY-16, and REY-30 were mapped to regions corresponding to the amino acids 175-1 99,253-282 and 288-3 12, respectively. MET-2 did not react with any of the peptides used. These results indicate that the present MAbs are directed against at least 4 distinct epitopes expressed on the Cterminal half of gp46. The binding of these MAbs to gp46 was specifically inhibited by sera from HTLV-I-infected individuals, but none of these MAbs inhibited the cell fusion activity of HTLV-I.