The present study has been formulated in order to detect an immunoreactive protein whose identification can play a major role in the early diagnosis of disease. The identified protein will be produced by recombinant methods and used for the recombinant protein based ELISA. A comparison was made between the developed method and the gold standard MAT test to evaluate the serodiagnosis potential of the protein. The protein profile, immunoblot and MALDI-TOF analysis was carried out to identify the immunoreactive protein. The immunoreactive protein identified was used to develop ELISA for the diagnosis of @entity2926 using @entity1 ' sera with various clinical manifestations. The immunoreactive protein was identified as @entity2928 GroEL chaperonin of molecular weight 60 kDa. The theoretical/experimental molecular weights, pI were found to be 58.5/60 kDa and 5.41/6, respectively. The overall results of the recombinant GroEL-IgM ELISAs showed cumulative sensitivity, specificity, positive predictive value, and negative predictive values of 90.6%, 94.9%, 94.6%, and 91.0%, respectively. The performance of such ELISA appeared better than that of any other serological tests previously evaluated for the diagnosis of @entity2926 in India. Thus, a highly conserved and immunogenic outer exposed GroEL protein during infection clearly merits further use in the serodiagnosis of @entity2926 .

Surface-associated Hsp60 chaperonin of XXXX serovar Autumnalis N2 strain as an immunoreactive protein.

@entity1 :: ('9606', 'Species') :: ['patients'] @entity2928 :: ('173', 'Species') :: ['Leptospira'] @entity2926 :: ('MESH:D007922', 'Disease') :: ['leptospirosis']
@entity2928 :: (173,Species) :: ['Leptospira interrogans']
