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Predicted structure and surface localization of the SmTSP-2 tetraspanin vaccine antigen from S. mansoni and fermentation and subsequent purification of.

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Presentation on theme: "Predicted structure and surface localization of the SmTSP-2 tetraspanin vaccine antigen from S. mansoni and fermentation and subsequent purification of."— Presentation transcript:

1 Predicted structure and surface localization of the SmTSP-2 tetraspanin vaccine antigen from S. mansoni and fermentation and subsequent purification of the recombinant protein. Predicted structure and surface localization of the SmTSP-2 tetraspanin vaccine antigen from S. mansoni and fermentation and subsequent purification of the recombinant protein. (A) SmTSP-2 is predicted to span the membrane four times, presenting small (EC-1) and large (EC-2) extracellular loops to the external environment. (B) Antibodies to recombinant SmTSP-2 EC-2 localized the expression to the tegument outer membrane of adult S. mansoni. (Reprinted from reference 147 with permission from Macmillan Publishers Ltd.) (C) Fermentation of recombinant SmTSP-2 EC-2 as a secreted protein in the yeast Pichia pastoris produces recombinant protein at yields in excess of 100 mg/liter of purified protein (M. Tran and A. Loukas, unpublished data). (D) Lane 1, molecular weight markers; lane 2, supernatant from yeast culture expressing SmTSP-2 EC-2; lanes 3 to 6, eluates from immobilized metal-affinity chromatography column containing purified recombinant SmTSP-2 EC-2. Donald P. McManus, and Alex Loukas Clin. Microbiol. Rev. 2008; doi: /CMR


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