Type-independent detection of foot-and-mouth disease virus by monoclonal antibodies that bind to amino-terminal residues of capsid protein VP2

The characterization of monoclonal antibodies raised against the foot-and-m outh disease virus isolates A22 Iraq/1964, Asia1 Shamir-Israel/1989, and SA T1 Zimbabwe/1989 with regard to neutralizing activity and sensitivity of th eir epitopes for treatment with trypsin, resulted in the identification of one non-neutralizing antibody in each panel that binds to a trypsin-sensiti ve epitope. Furthermore, each of these antibodies recognized 27 isolates of different provenance. representative of six serotypes. These antibodies ar e recommended for type-independent antigen detection by ELISA. The epitopes for these antibodies reside at the intertypically conserved N-terminus of capsid protein VP2. The two are specified by the lysines at positions two a nd three, but differ from each other as indicated by the variable heavy cha in sequences of their antibodies. (C) 2001 Elsevier Science B.V. All rights reserved.