Serological discrimination between HTLV-I and HTLV-II antibodies by elisa using synthetic peptides as antigens

✍ Scribed by Yukiko Washitani; Naotaka Kuroda; Hiroshi Shiraki; Youko Nishimura; Kazunari Yamaguchi; Kiyoshi Takatsuki; Leonor P. Fernando; Chyang T. Fang; Hiroyuki Kiyokawa; Yoshiaki Maeda

• Book ID: 102278360
• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: French
• Weight: 476 KB
• Volume: 49
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910490204

✦ Synopsis

Abstract

Using the peptides from amino acids 100‐130 of the HTLV‐I gag protein, 175‐199 of the HTLV‐I env protein and the corresponding peptides of HTLV‐II (amino acids 106 to 135 of the gag protein and 171 to 196 of the env protein), we tested for reactivity against antibodies by enzyme immunoassay in sera from HTLV‐I and HTLV‐II carriers. The peptides derived from the env proteins have high specificity for antibody binding. The peptide based on amino acids 175‐199 of HTLV‐I reacted with antibodies in sera from all HTLV‐I carriers, and the peptide composed of amino acids 171‐196 of HTLV‐II reacted with antibodies in sera from all HTLV‐II carriers. For the peptides derived from the gag proteins, we observed some cross‐reactivity in sera from persons with anti‐HTLV‐I and anti‐HTLV‐II, due to antibody binding to the peptide corresponding to 12 amino acids from the C‐terminal end of the gag protein. Separate enzyme immunoassays that used the four synthetic peptides as antigens clearly distinguished between serum with antibodies to HTLV‐I or HTLV‐II in various individuals and excluded false positive results using the particle agglutination assay that used a whole‐virus lysate of HTLV‐I as antigen.