• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Journal of Bacteriology >Antigenic diversity of the S-layer proteins from pathogenic strains of Aeromonas hydrophila and Aeromonas veronii biotype sobria.
【2h】

Antigenic diversity of the S-layer proteins from pathogenic strains of Aeromonas hydrophila and Aeromonas veronii biotype sobria.

机译：嗜水气单胞菌和veronii veronii生物型索氏菌致病株的S层蛋白的抗原多样性。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The antigenic relatedness of paracrystalline surface array proteins with subunit molecular weights of approximately 52,000 from isolates of Aeromonas hydrophila and Aeromonas veronii biotype sobria belonging to a single heat-stable serogroup was examined. Enzyme-linked immunosorbent assay and immunoblotting with two different polyclonal antisera against surface exposed and non-surface-exposed epitopes of the S-layer protein from A. hydrophila TF7 showed that the S-layer proteins of the mesophilic aeromonads were antigenically diverse. NH2-terminal amino acid sequence analysis of four antigenically different proteins showed that while the proteins were structurally related, they differed in primary sequence. Absorption experiments with heterologous live cells showed that cross-reactive epitopes were in non-surface-exposed regions of the S-layer proteins, while absorption with homologous live cells showed that the immunodominant epitopes of the S-layer protein of strain TF7 were strain specific and exposed on the surface of the native, tetragonal array produced by this strain. Proteolytic digestion of the TF7 S-layer protein with trypsin, chymotrypsin, or endoproteinase Glu-C produced an amino-terminal peptide of approximate Mr 38,000 which was refractile to further proteolytic cleavage under nondenaturing conditions. This peptide carried the immunodominant surface-exposed region of the protein, and chemical cleavage with cyanogen bromide further mapped the portion of these surface-exposed epitopes to a peptide of approximate Mr 26,000, part of which maps within the Mr 38,000 protease-resistant NH2-terminal peptide.
机译：从属于单个热稳定血清群的嗜水气单胞菌和veronii veronii生物型索氏菌的分离物中检测了亚基分子量约为52,000的亚晶面表面阵列蛋白的抗原相关性。酶联免疫吸附测定和针对嗜水链球菌TF7的S层蛋白的表面暴露和非表面暴露的表位的两种不同的多克隆抗血清进行的免疫印迹表明，嗜温气单胞菌的S层蛋白在抗原上是多种多样的。四种抗原性不同的蛋白质的NH2-末端氨基酸序列分析表明，尽管蛋白质在结构上相关，但它们的一级序列不同。异源活细胞的吸收实验表明，交叉反应的抗原决定簇位于S层蛋白的非表面暴露区域，而同质活细胞的吸收表明，菌株TF7的S层蛋白的免疫显性抗原决定簇是菌株特异性的。并暴露在由该菌株产生的天然四边形阵列的表面上。用胰蛋白酶，胰凝乳蛋白酶或内切蛋白酶Glu-C对TF7 S层蛋白进行蛋白水解消化，产生的氨基末端肽大约为38,000，在非变性条件下可进行进一步蛋白水解切割。该肽带有蛋白质的免疫显性表面暴露区域，并且用溴化氰化学切割进一步将这些表面暴露表位的部分映射到大约26,000 Mr的肽，其中一部分在抗Mr 38,000的NH2-内定位末端肽。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号