Comparative Proteomic Analysis of Hydrogen Peroxide-Induced Protein Expression in Streptococcus pneumoniae D39

Author:

Lee Sungkyoung1ORCID,Lee Myoung-Ro2,Bae Songmee3ORCID,Kwak Min-Kyu4ORCID

Affiliation:

1. Division of Bacterial Disease Research, Center for Infectious Disease Research, Korea National Institute of Health, Korea Disease Control and Prevention Agency, Cheongju-si, Chungcheongbuk-do, 28160, Korea

2. Division of Vectors and Parasitic Diseases, Center for Laboratory Control of Infectious Diseases, Korea Disease Control and Prevention Agency, Cheongju-si, Chungcheongbuk-do, 28160, Korea

3. Division of Antimicrobial Resistance, Research Center for Infectious Disease Research, Korea National Institute of Health, Korea Disease Control and Prevention Agency, Cheongju-si, Chungcheongbuk-do, 28160, Korea

4. Laboratory of Microbial Physiology and Biotechnology, Department of Food and Nutrition, Institute of Food and Nutrition Science, Eulji University, Gyeonggi-do, 13135, Korea

Abstract

Background: Streptococcus pneumoniaeis a leading cause of human respiratory tract infection. Despite the lack of activities of antioxidative enzymes, including cytochromes, hemoproteins, and peroxidases/catalases, traits conferring the aerotolerant-anaerobic growth of this bacterium are conserved, with the high efficacy of antioxidative actions, in an oxygen-rich environment. Objective: Through proteome analysis, this study's intention was to evaluate differentially expressed proteins and/or gene products modeled in a highly virulent strain, S. pneumoniae D39, exogenously- treated with millimolar concentrations of H2O2. Method: For two-dimensional gel electrophoresis (2-DE) analysis, following one dimensional isoelectric focusing with an immobilized pH gradient of pH 4-7, the most significantly mobilized proteins expressed were separated by SDS-PAGE in the second dimension. With a total of 431 protein spots detected, certain proteins were excised, in-gel trypsin digested, and analyzed by combination with MALDI-TOF and LC-ESI-MS/MS for mass spectrometric peptide mapping and protein identification. Utilizing mass spectrometry analysis of spots excised from 2-DE, the selected protein spots were identified with a variety of databases and MASCOT. Results: With the aid of comparisons to proteome reference maps, the most differentially expressed 38 proteins, those with approximately 1.4-fold or more increase and/or decrease or with multiple isoforms exhibiting variable pI values, were induced by treatment of exogenous 2 mM H2O2.The identified proteins were seen to be involved in pneumococcal pathogenesis and primary metabolism, amongst others. Conclusion: This is the first study to convincingly document proteomic information associated with pathophysiological adaptation under the given oxidative conditions, and corresponding potential antioxidative mechanisms, in S. pneumoniae.

Funder

Pathogenic Proteome Management Program-NIH Korea

Korea Centers for Disease Control and Prevention

Publisher

Bentham Science Publishers Ltd.

Subject

Molecular Biology,Biochemistry

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3