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LTB consisted of five identical polypeptides and, as a pentameric form, has been demonstrated to bind to the GM1 ganglioside at cellular surface. The recombinant LTB has attracted much attention due to its non-toxicity and potential as a strong immunogenic antigen and immuno adjuvant for both system and mucosal immune responses. Actinobacillus pleuropneumoniae is the causal agent of swine pleuropneumoniae, a disease resulting in morbidity and mortality of pigs and accordingly economic losses within the swine industry.
Toxins (APX) produced by A. pleuropneumoniae appear to be important virulence factors of swine pleuropneumoniae. In order to use S.cerevisiae for effective delivery of APX to the gut-associated lymphoid tissue, a chimeric APX fused with LTB subunit (LTB-APX) was constructed and tested for the oligimerization, which enables the chimeric complex to bind the intestinal
membrane GM1-ganglioside receptor. Westhern blot ananlysis and ELISA indicated that a chimeric fusion protein was produced in recombinant S.
cerevisiae. However, assembly into the native pentameric structure did not occur probably due to the stearic hinderance caused by the increased size of LTB-APX fusion construct. Therefore, co-expression strategy using episomal and integrative vectors for LTB and LTB-APX, respectively, was suggested for the oligomerization of chimeric LTB-APX fusion construct.