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Characteristics of Vibrio cholerae proteinases: potential, candidate vaccine antigens

机译：霍乱弧菌蛋白酶的特征：潜在的候选疫苗抗原

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Vibrio cholerae extracellular proteinases (proteases) have been studied as potential candidate antigens for acellular cholera vaccines. Proteinases from V cholerae NCTC 10732 were prepared from batch culture either by ammonium sulphate precipitation and G100 Sephadex gel filtration or by isoelectric focusing (IEF). Proteinase activity was at a maximum level after 24h, coincident with the late exponential phase and early stationary phase. Three major IEF peaks of activity were resolved with specific activities in the range 17.2-195 EU ml(-1) mg(-1). Sodium dodecyl sulphate-polyacrylamide gel electrophoreses (SDS-PAGE) of these fractions revealed 42, 45, 57 and 75 kDa bands in which proteinase activity was demonstrable. Peptide digest analysis suggested different catalytic specificities for each proteinase fraction. Metalloproteinase and serine proteinase inhibitors, alpha(2)-macroglobulin (alpha(2)-M), the thiol proteinase inhibitor and N-ethylmaleimide inhibited the proteinases. The proteinases nicked Escherichia coli heat-labile toxin to yield catalytically active sub-units, confirmed by the measurement of intrinsic ADP-ribosylation activity. The possible value of these putative V. cholerae antigens in an acellular vaccine is discussed.
机译：霍乱弧菌胞外蛋白酶（蛋白酶）已被研究为脱细胞霍乱疫苗的潜在候选抗原。霍乱弧菌NCTC 10732的蛋白酶是通过分批培养通过硫酸铵沉淀和G100 Sephadex凝胶过滤或通过等电聚焦（IEF）制备的。蛋白酶活性在24h后达到最高水平，与指数后期和固定早期相一致。通过在17.2-195 EU ml（-1）mg（-1）范围内的比活可以分辨出三个主要的IEF活性峰值。这些馏分的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）显示出42、45、57和75 kDa的条带，其中的蛋白酶活性可证实。肽消化分析表明每种蛋白酶组分的催化特异性不同。金属蛋白酶和丝氨酸蛋白酶抑制剂，α（2）-巨球蛋白（alpha（2）-M），硫醇蛋白酶抑制剂和N-乙基马来酰亚胺抑制蛋白酶。蛋白酶切割了大肠杆菌的热不稳定毒素，产生了催化活性的亚基，这一点已通过内在ADP-核糖基化活性的测定得到证实。讨论了这些推定的霍乱弧菌抗原在无细胞疫苗中的可能价值。

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