• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>RSC Advances >Rational design, preparation and characterization of recombinant Ag85B variants and their glycoconjugates with T-cell antigenic activity against Mycobacterium tuberculosis
【24h】

Rational design, preparation and characterization of recombinant Ag85B variants and their glycoconjugates with T-cell antigenic activity against Mycobacterium tuberculosis

机译：重组Ag85B变体的合理设计，制备和表征及其对结核分枝杆菌的T细胞抗原活性的血糖缀合物

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Tuberculosis is the deadliest infectious disease in the world. The variable efficacy of the current treatments highlights the need for more effective agents against this disease. In the past few years, we focused on the investigation of antigenic glycoconjugates starting from recombinant Ag85B (rAg85B), a potent protein antigen from Mycobacterium tuberculosis. In this paper, structural modifications were rationally designed in order to obtain a rAg85B variant protein able to maintain its immunogenicity after glycosylation. Lysine residues involved in the main T-epitope sequences (namely, K30 and K282) have been substituted with arginine to prevent their glycosylation by a lysine-specific reactive linker. The effectiveness of the mutation strategy and the detailed structure of resulting neo-glycoconjugates have been studied by intact mass spectrometry, followed by peptide and glycopeptide mapping. The effect of K30R and K282R mutations on the T-cell activity of rAg85B has also been investigated with a preliminary immunological evaluation performed by enzyme-linked immunospotting on the different variant proteins and their glycosylation products. After glycosylation, the two variant proteins with an arginine in position 30 completely retain the original T-cell activity, thus representing adequate antigenic carriers for the development of efficient glycoconjugate vaccines against tuberculosis.
机译：结核病是世界上最致命的传染病。目前治疗的可变功效突出了对这种疾病更有效的药剂的需要。在过去的几年中，我们专注于从重组Ag85b（Rag85b）开始的抗原糖缀合物，从结核分枝杆菌的有效蛋白质抗原开始研究。在本文中，结构修改是合理设计的，以获得能够在糖基化后保持其免疫原性的RAG85B变体蛋白。参与主T表序列（即K30和K282）的赖氨酸残基已被精氨酸取代，以通过赖氨酸特异性的反应性接头防止它们的糖基化。通过完整的质谱法研究了突变策略的有效性和所得到的新糖缀合物的详细结构，然后是肽和糖肽测绘。还研究了K30R和K282R突变对RAG85B的T细胞活性的影响，并通过酶联免疫分散在不同变体蛋白及其糖基化产物上进行了初步免疫学评估。在糖基化之后，两个具有精氨酸的两种变体蛋白质在位30完全保留原始T细胞活性，从而代表足够的抗原载体，用于开发有效的糖凝胶疫苗对结核病的疫苗。

著录项

  • 来源
    《RSC Advances》 |2018年第41期|共10页
  • 作者

    Rinaldi Francesca; Tengattini Sara; Piubelli Luciano; Bernardini Roberta; Mangione Francesca; Bavaro Teodora; Paone Gregorino; Mattei Maurizio; Pollegioni Loredano; Filice Gaetano; Temporini Caterina; Terreni Marco;

  • 作者单位

    Univ Pavia Dept Drug Sci Viale Taramelli 12 I-27100 Pavia Italy;

    Univ Pavia Dept Drug Sci Viale Taramelli 12 I-27100 Pavia Italy;

    Univ Insubria Dept Biotechnol &

    Life Sci Via Dunant 3 I-21100 Varese Italy;

    Univ Roma Tor Vergata Dept Biol Via Montpellier 1 I-00133 Rome Italy;

    IRCCS San Matteo Hosp Fdn Microbiol &

    Virol Unit Viale Camillo Golgi 19 I-27100 Pavia Italy;

    Univ Pavia Dept Drug Sci Viale Taramelli 12 I-27100 Pavia Italy;

    Sapienza Univ Rome Dept Cardiovasc Resp Nephrol Anesthesiol &

    Geriat Piazzale Aldo Moro 5 I-00185 Rome Italy;

    Univ Roma Tor Vergata Dept Biol Via Montpellier 1 I-00133 Rome Italy;

    Univ Insubria Dept Biotechnol &

    Life Sci Via Dunant 3 I-21100 Varese Italy;

    Univ Pavia Dept Internal Med &

    Therapeut Viale Camillo Golgi 19 I-27100 Pavia Italy;

    Univ Pavia Dept Drug Sci Viale Taramelli 12 I-27100 Pavia Italy;

    Univ Pavia Dept Drug Sci Viale Taramelli 12 I-27100 Pavia Italy;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

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