The polymorphism of Theileria buffeli major surface protein associate with their clinical signs in holstein in Korea / 대한수의학회지

Theileria (T.) buffeli (formerly T. sergenti/T. orientalis) is the major hemo-protozoan distributed in the Far East Asian countries such as Korea, China and Japan. It is responsible for the clinical symptoms of anorexia, ateliosis, anemia, fever and icterus. It also causes abortion and sudden death under severe cases, resulting in economic losses for many livestock farms. The objective of this study was to analyze the genetic diversity of the major surface protein (Msp) gene in T. buffeli in Holstein in Korea, and we characterized the association of the diversification of the Msp gene and its relationship with the pathogenicity of Theileria. For this, complete blood counts and Theileria PCR sequence analysis were performed from 57 Holstein in Jeju Island. A total of 26 PCR positive Holstein (16 anemic and 10 non-anemic) were then randomly selected based on 18s rRNA sequence typing of the Theileria Msp gene. The DNA sequence of the T. buffeli Msp gene in Holstein showed 99.0%, 99.2%, 99.9%, 99.5%, 98.7%, 98.4% and 98.4% homology with T. sergenti, Theileria spp., T. sergenti, Theileria spp., Theileria spp., Theileria spp. and Theileria spp., respectively. The result showed a genetic variation of 57.7% (type I), 3.8% (type II), 15.4% (type III), 7.7% (type IV), 13.5% (type V) and 1.9% (type VI). Type I is the most frequent type in both anemic and non-anemic Holstein while type II was found in only non-anemic Holstein. This results of our study help confirm the diversity of Msp gene types and demonstrate that the gene type distribution of Msp genes varies among Theileria-infected Holstein in Jeju Island.

Functional Characterization of the Major Outer Membrane Protein ( MspTL ) of Treponema lecithinolyticum

Treponema lecithinolyticum is known to be associated with rapidly progressive periodontitis. The full-length gene encoding the major surface protein MspTL of this organism was cloned and expressed by using the expression vector pQE30. Recombinant Msp TL (rMsp TL) protein was purified and functionally characterized. Msp TL was one of several T. lecithinolyticum surface proteins that bound to cultured human gingival fibroblasts (HGFs). As well, it strongly induced IL-6 production by HGFs. These observations suggest that MspTL contributes to pathogenesis of periodontitis by adhesion to host cells and by induction of the proinflammatory cytokine IL-6.