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AIM To determine the function and cellular localization of GS-encoded proteins and to assess their potentialas drug targets and vaccine components.METHODS Bioinformatics software was used to predict the function of GS-encoded proteins and theirlocation within MAP. Protein modelling software was used to build protein structures.RESULTS The gene gsa is a truncated glycosyl transferase and probably non-functional. gsbA and gsbBproduce GDP-fucose which is methylated by gsc and acetylated by mpa. gsd is a fucosyl transferase whichattaches fucose to subterminal rhamnose on cell surface glycopeptidolipid. gsa, gsbA and gsbB and gsc arelocated within the cytoplasm. mpa is embedded in the plasma membrane with 10 transmembrane regions anda conspicuous extracellular loop. gsd is lipid-linked and predicted to localize to the microbial cell surface.CONCLUSION GS encodes the biosynthetic machinery to give MAP a surface coat of methylated andacetylated fucose which may contribute to its protease-resistant nature and ability to minimize immunerecognition. The gsbA/gsbB operon and gsd are promising drug targets and gsd is a good candidatecomponent of a new class of anti-MAP vaccines.
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肠道病毒71疫苗候选株H3-TY的遗传稳定性研究
了解肠道病毒71(EV71)疫苗候选株H3-TY的遗传稳定性。方法选取EV71疫苗候选株H3-TY种子库中的6个子代病毒，提取RNA，对其VP1基因进行RT-PCR扩增、克隆、序列测定，然后对所获基因序列进行同源性分析并计算同源率。结果H3-TY的6个子代病毒VP1基因之间核苷酸同源性介于99.6％ ～99.8％，氨基酸同源性为100.0％，主要抗原决定簇的氨基酸序列完全一致。结论H3-TY种子库中6代病毒的VP1基因之间高度同源，主要抗原决定簇稳定遗传。
