Mycobacterium avium subsp.
paratuberculosis (Map) contains PE family
antigens which are
Proline and
glutamic acid rich and may play important role as T-cell
antigens. In the present study, the Map 1507 ORF encoding 9.7 kDa PE
protein was amplified by polymerase chain reaction and cloned into E. coli vector pQE30 UA. The recombinant plasmid designated as pQ PE was transformed into E. coli
M15 cells and induced with
IPTG revealed the high level expression of 11.9 kDa His-fusion
protein as estimated by migration in 15 %
sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Recombinant PE
protein was purified by Ni-NTA
agarose chromatography. Polyclonal
antibodies raised against purified recombinant PE
protein reacted with expressed PE
protein as well as with Map sonicate. The recombinant PE
protein was also recognized by serum from goat with clinical
paratuberculosis. The
protein elicited significant delayed type
hypersensitivity (DTH) skin reaction in mice sensitized with Map. The results indicated that the recombinant PE
protein of Map was associated with T-cell response.