Detection of Anaplasma antibodies in wildlife and domestic species in wildlife-livestock interface areas of Kenya by major surface protein 5 competitive inhibition enzyme-linked immunosorbent assay.

The seroprevalence of Anaplasma antibodies in wildlife (eland, blue wildebeest, kongoni, impala, Thomson's gazelle, Grant's gazelle, giraffe and plains zebra) and domestic animal (cattle, sheep and goat) populations was studied in wildlife/livestock interface areas of Kenya. Serum samples were analyzed by competitive inhibition enzyme-linked immunosorbent assay (CI-ELISA), using a recombinant antigen (MSP-5) from Anaplasma marginale surface membrane. A monoclonal antibody, FC-16, was used as the primary antibody, while anti-mouse conjugated to horseradish peroxidase was used as the secondary antibody. The results indicate a high seroprevalence in both wildlife and livestock populations, in contrast to earlier reports from Kenya, which indicated a low seroprevalence. The differences are attributed to the accurate analytical method used (CI-ELISA), as compared with agglutination techniques, clinical signs and microscopy employed by the earlier workers.

Monoclonal antibody binding to a surface-exposed epitope on Cowdria ruminantium that is conserved among eight strains.

Monoclonal antibodies (MAb) binding to Cowdria ruminantium elementary bodies (EB) were identified by enzyme-linked immunosorbent assay, and surface binding of one MAb (446.15) to intact EB was determined by immunofluorescence, immunogold labeling, and transmission electron microscopy. MAb 446.15 bound an antigen of approximately 43 kDa in immunoblots of eight geographically distinct strains. The MAb did not react with Ehrlichia canis antigens or uninfected bovine endothelial cell lysate and may be useful in diagnostic assays and vaccine development.

Monoclonal antibody differentiation of Mycoplasma mycoides subsp. mycoides small-colony strains causing contagious bovine pleuropneumonia from less important large-colony strains.

Monoclonal antibody (MAb) PK-2 inhibited the in vitro growth of nine Mycoplasma mycoides subsp. mycoides small-colony strains. In contrast to the results with polyclonal antisera, growth inhibition by MAb PK-2 was specific for M. mycoides subsp. mycoides small-colony strains and constituted a reliable means of distinguishing them from other mycoplasmas.

Monoclonal antibody E8-18 identifies an integral membrane surface protein unique to Mycoplasma capricolum subsp. capripneumoniae.

Monoclonal antibody (MAb) E8-18 reacted with four isolates of Mycoplasma capricolum subsp. capripneumoniae in Western blots identifying an epitope on a 24 kDa antigen (p24). MAb E8-18 did not react with 11 isolates belonging to four other Mycoplasma species or subspecies closely related to M. capricolum subsp. capripneumoniae. A combination of trypsin treatment of intact organisms and detergent-phase partitioning revealed p24 to be an integral M. capricolum subsp. capripneumoniae surface membrane protein.

A Mycoplasma strain F38 growth-inhibiting monoclonal antibody (WM-25) identifies an epitope on a surface-exposed polysaccharide antigen.

Monoclonal antibody (MAb) WM-25 differentiates by in vitro growth inhibition Mycoplasma capricolum subsp. capripneumoniae (Mycoplasma strain F38), which causes contagious carpine pleuropneumonia, from other Mycoplasma spp. (F. R. Rurangirwa, T. C. McGuire, A. J. Musoke, and A. Kibor, Infect. Immun. 55:3219-3220, 1987). The antigen identified by MAb WM-25 was isolated from solubilized Mycoplasma strain F38 organisms by MAb WM-25 affinity chromatography and was stained with Schiff's reagent, but not with Coomassie blue, after separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Treatment of purified F38 polysaccharide with periodate abolished binding with MAb WM-25, and MAb WM-25 binding was blocked with laminarin, a complex oligosaccharide with beta(1-->3) sugar linkages. Purified F38 polysaccharide blocked both growth inhibition and agglutination of live F38 organisms caused by MAb WM-25 and rabbit antiserum to F38 organisms. The results in this paper demonstrate that MAb WM-25 binds a periodate-sensitive epitope on the F38 polysaccharide which is also exposed on the surface of Mycoplasma strain F38. Because MAb WM-25 also causes in vitro growth inhibition of F38, the reactive polysaccharide epitope may induce protective immune responses.

Preliminary field test of lyophilised contagious caprine pleuropneumonia vaccine.

Fifty goats were immunised in the field against contagious caprine pleuropneumonia (CCPP) using a single dose (0.15 mg) of lyophilised, saponin killed Mycoplasma strain F38. Two months after vaccination, these goats together with 50 unimmunised control goats were challenged by contact with goats experimentally infected with CCPP. Twelve vaccinates and 14 controls died of diarrhoea due to salmonella infection during the first two weeks after challenge. The remaining immunised goats (38) with the exception of two goats which had elevated temperatures were protected from CCPP. Of the remaining 36 control goats, 30 contracted CCPP at a mean of 39 (+/- 14.3 SD) days after challenge and 27 of them died. These results show that the lyophilised killed F38 vaccine conferred 100 per cent protection against mortality and 95 per cent protection against clinical disease caused by Mycoplasma species strain F38.

Thyroid function as assessed by routine laboratory tests of workers with long-term lead exposure.

Thyroid function was studied in 176 male workers occupationally exposed to lead. The mean blood lead concentration of the workers was 2.70 (SD 1.15, range 0.70-6.45) mumol/l. The mean duration of lead exposure was 7.6 (range 0.1-20) years. The total thyroxine (T4), free thyroxine (FT4), total triiodothyronine (T3), and thyrotropin concentrations in serum were similar in the workers in the low and high blood lead categories. In regression equations the duration of lead exposure had a weak but significant negative association with T4 and FT4, and this association was particularly pronounced when the analyses were restricted to workers with the most intense lead exposure over time. Thus, the results suggest that thyroid function might be depressed as a result of intense long-term lead exposure.