Prohibitins comprise a highly conserved family of proteins
implicated in important cellular processes. We obtained the complete CPB prohibitin-1 DNA coding
sequence of 828 pb, in silico translated into a 276-amino acid protein. The analysis at the amino acid level
showed that the protein contains a prohibitin-homology domain (Band7_prohibitin, cd03401) conserved
among prohibitin proteins. A striking feature of the CPB identified prohibitin-1 is the predicted presence
of cadherin elements, potential binding sites for Cry toxins described in other Bt susceptible insects. We
also showed that CPB prohibitin-1 protein partitioned into both, detergent soluble and insoluble membrane
fractions, as well as a prohibitin-2 homologous protein, previously reported to form functional
complexes with prohibitin-1 in other organisms.