Monoclonal antibody to the aminotelopeptide of type II collagen: loss of the epitope after stromelysin digestion.

A monoclonal antibody was prepared to the aminotelopeptide of type II collagen after immunization of DBA/1 mice with lathyritic type II collagen and subsequent screening for antibodies that recognize lathyritic but not pepsin-digested type II collagen. One antibody (called 5B2) was identified that recognized a short peptide sequence in the aminotelopeptide of chicken type II collagen but did not recognize other collagen types. Further characterization of the epitope was achieved using a Multipin system and the epitope was localized to a short linear sequence of six amino acids. The antibody recognized type II collagen from a variety of species including man and mouse. The epitope for 5B2 was found to be susceptible to cleavage with recombinant stromelysin without cleavage of the major collagen triple helix. Comparison was made between MAb 5B2 and two other antibodies (called MAb 2B1 and MAb 6B3) that recognize separate epitopes located along the triple helix of the type II collagen molecule.