Structural genomics studies of human caries pathogen Streptococcus mutans

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• 作者：Lanfen Li (1)
  Jie Nan (1) (3)
  Dan Li (1) (4)
  Erik Brostromer (1) (5)
  Zixi Wang (1)
  Cong Liu (1) (4)
  Qiaoming Hou (1)
  Xuexin Fan (1)
  Zhaoyang Ye (1)
  Xiao-Dong Su (1) (2)
  
• 关键词：Structural genomics ; Lab automation ; HTP method development ; Protein crystallization ; Streptococcus mutans
• 刊名：Journal of Structural and Functional Genomics
• 出版年：2014
• 出版时间：September 2014
• 年：2014
• 卷：15
• 期：3
• 页码：91-99
• 全文大小：1,372 KB
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• 作者单位：Lanfen Li (1)
  Jie Nan (1) (3)
  Dan Li (1) (4)
  Erik Brostromer (1) (5)
  Zixi Wang (1)
  Cong Liu (1) (4)
  Qiaoming Hou (1)
  Xuexin Fan (1)
  Zhaoyang Ye (1)
  Xiao-Dong Su (1) (2)
  
  1. State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, 100871, China
  3. Department of Cell and Molecular Biology, Uppsala University, 75124, Uppsala, Sweden
  4. UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, CA, 90095, USA
  5. Str枚m & Gulliksson AB, 220 07, Lund, Sweden
  2. Biodynamic Optical Imaging Center (BIOPIC), Peking University, Beijing, 100871, China
  
• ISSN：1570-0267

文摘

Gram-positive bacterium Streptococcus mutans is the primary causative agent of human dental caries. To better understand this pathogen at the atomic structure level and to establish potential drug and vaccine targets, we have carried out structural genomics research since 2005. To achieve the goal, we have developed various in-house automation systems including novel high-throughput crystallization equipment and methods, based on which a large-scale, high-efficiency and low-cost platform has been establish in our laboratory. From a total of 1,963 annotated open reading frames, 1,391 non-membrane targets were selected prioritized by protein sequence similarities to unknown structures, and clustered by restriction sites to allow for cost-effective high-throughput conventional cloning. Selected proteins were over-expressed in different strains of Escherichia coli. Clones expressed soluble proteins were selected, expanded, and expressed proteins were purified and subjected to crystallization trials. Finally, protein crystals were subjected to X-ray analysis and structures were determined by crystallographic methods. Using the previously established procedures, we have so far obtained more than 200 kinds of protein crystals and 100 kinds of crystal structures involved in different biological pathways. In this paper we demonstrate and review a possibility of performing structural genomics studies at moderate laboratory scale. Furthermore, the techniques and methods developed in our study can be widely applied to conventional structural biology research practice.