Objective  To investigate the cross-immunoreactivity between the serine proteases derived from Anopheles dirus and Manduca.    Methods  Bioinformatic analysis were carried out to determine the conservation of serine protease amino acid sequences among different insects

especially its similarity of the 2 above-mentioned insects. Serine protease of Anopheles dirus was expressed in E. coli by PinPoint

TM

Xa-1 T-vector. Western blotting was used to examine the cross-immunoreactiviy between the expression product and the antiserum against serine protease of Manduca.   Results  High similarity was found in serine protease amino acid sequences of different insect

includin

g Anopheles dirus and Manduca. Serine protease of Anopheles was successfully expressed in E. coli. Western blot analysis showed that the expression product was recognized by the antiserum.   Conclusion  There is cross-immunoreactivity between serine protease of Anopheles dirus and Manduca. So it is feasible to study serine protease of Anopheles dirus with antiserum against Manduca serine protease.