Antibody Reactivity to Omp31 fromBrucella melitensisin Human and Animal Infections by Smooth and Rough Brucellae

Abstract
Group 3 of outer membrane proteins (OMPs) ofBrucellaincludes Omp25 and Omp31, which share 34% identity. Omp25 is highly conserved inBrucellaspecies, and Omp31 is present in allBrucellaspecies, exceptBrucella abortus. Antibodies toBrucella melitensisOmp31 have been sought only in infected sheep, and Western blotting of sera from infected sheep did not reveal anti-Omp31 reactivity. We obtained recombinant purified Omp31 (B. melitensis) and tested its recognition by sera from humans and animals suffering from brucellosis by an indirect enzyme-linked immunosorbent assay (ELISA). Serum samples from 74 patients, 57 sheep, and 47 dogs were analyzed; brucellosis was confirmed by bacteriological isolation in all ovine and canine cases and 31 human cases of brucellosis. Thirty-five patients (47%) were positive for antibodies to Omp31, including seven cases ofBrucella suisinfection, two cases ofB. abortusinfection, and three cases ofB. melitensisinfection. Of 39 sheep naturally infected withB. melitensis(biovars 1 and 3), 23 (59%) were positive for antibodies to Omp31. Anti-Omp31 antibodies were also detected in 12 of 18 rams (67%) in whichBrucella oviswas isolated from semen. Antibodies to Omp31 were also found in 41 (87%) of the 47 dogs, including 13 with recent infection. These results suggest that an indirect ELISA using recombinant purified Omp31 fromB. melitensiswould be of limited value for the diagnosis of human and animal brucellosis. Nevertheless, the potential usefulness of this antigen in combination with other recombinant proteins fromBrucellashould not be dismissed.

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