• Title/Summary/Keyword: pathogen proteomics

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Proteomics of plant-fungal pathogen interaction: an overview (식물과 곰팡이 병원균과의 상호작용에 대한 프로테오믹스 최근 연구 동향)

  • Kim, Jin Yeong;Lee, So Eui;Oh, Ha Ram;Choi, In Soo;Kim, Yong Chul;Kim, Sun Tae
    • Journal of Plant Biotechnology
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    • v.41 no.1
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    • pp.1-9
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    • 2014
  • So far it has been generally considered that proteomic approaches are very useful for studying plant-microbes interaction. In this review, recent studies based on papers published from 2010 to 2013 have investigated proteomics analysis in various interaction during plant-fungal pathogen infection by means of gel-based proteomics coupled with mass spectrometry (MS)-based analysis. In rice, three papers focused on rice-Magnaporthe oryzae interaction were mainly reviewed in this study. Interestingly, another study showed proteomic changes in rice inoculated with Puccinia triticina, which is not only an fungal pathogen in wheat and but also results to the disease resistance with non-host defense manner in rice. Additionally, proteomics analysis has been widely subjected to understand defense mechanism during other crops (wheat, tomato, strawberry and mint) and their fungal pathogen interaction. Crops inoculated are analyzed to identify differentially regulated proteins at various tissues such as leaf and apoplast using 2-DE analysis coupled with various MS approaches such as MALDI-TOF MS, nESI-LC-MS/MS and MudPIT, respectively. Taken together, this review article shows that proteomics is applicable to various organisms to understand plant-fungal pathogen interaction and will contribute to provide important information for crop disease diagnosis and crop protection.

Proteomic Analysis of Shigella Virulence Effectors Secreted under Different Conditions

  • Liu, Xingming;Lu, Lilan;Liu, Xinrui;Liu, Xiankai;Pan, Chao;Feng, Erling;Wang, Dongshu;Niu, Chang;Zhu, Li;Wang, Hengliang
    • Journal of Microbiology and Biotechnology
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    • v.27 no.1
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    • pp.171-178
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    • 2017
  • A series of novel effector molecules secreted by the type three secretion system (T3SS) of Shigella spp. have been reported in recent years. In this study, a proteomic approach was applied to study T3SS effectors systematically. First, proteins secreted by the S. flexneri wild-type strain after Congo Red induction were separated and identified using two-dimensional electrophoresis to display the relative abundance of all kinds of early effectors for the first time. Then, a gene deletion mutant of known virulence repressor (OspD1) and a gene overexpressed mutant of two known virulence activators (MxiE and IpgC) were constructed and analyzed to discover potential late effectors. Furthermore, the supernatant proteins of gene deletion mutants of two known translocators (IpaB and IpaD), which would constantly secrete effectors, were also analyzed. Among all of the secreted proteins identified in our study, IpaH1.4, IpaH_5, and IpaH_7 have not been reported before. These proteomics data of the secreted effectors will be valuable to understand the pathogenesis of S. flexneri.

2DSpotDB: A Database for the Annotated Two-dimensional Polyacrylamide Gel Electrophoresis of Pathogen Proteins

  • Kim, Dae-Won;Yoo, Won-Gi;Lee, Myoung-Ro;Kim, Yu-Jung;Cho, Shin-Hyeong;Lee, Won-Ja;Ju, Jung-Won
    • Genomics & Informatics
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    • v.9 no.4
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    • pp.197-199
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    • 2011
  • The biological interpretation of two-dimensional (2D) gel electrophoresis experiments is a key step toward understanding the functions of biological systems. We here present a web-based integrated database, called 2DSpotDB, for the management of proteome data derived from several pathogens. The 2DSpotDB was established as a part of the management of a pathogen proteome project at the Korea National Institute of Health. The goals of the 2DSpotDB implementation are to store and define important pathogen genes, retrieve information obtained by 2D polyacrylamide gel electrophoresis and mass spectrometry, and create an integrated system to provide pathogen proteome information for biological scientists. This database currently contains 14 gels and information on 387 protein spots, among which 329 proteins were identified and annotated.

Proteomic Comparison of Gibberella moniliformis in Limited-Nitrogen (Fumonisin-Inducing) and Excess-Nitrogen (Fumonisin-Repressing) Conditions

  • Choi, Yoon-E;Butchko, Robert A.E.;Shim, Won-Bo
    • Journal of Microbiology and Biotechnology
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    • v.22 no.6
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    • pp.780-787
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    • 2012
  • The maize pathogen Gibberella moniliformis produces fumonisins, a group of mycotoxins associated with several disorders in animals and humans, including cancer. The current focus of our research is to understand the regulatory mechanisms involved in fumonisin biosynthesis. In this study, we employed a proteomics approach to identify novel genes involved in the fumonisin biosynthesis under nitrogen stress. The combination of genome sequence, mutant strains, EST database, microarrays, and proteomics offers an opportunity to advance our understanding of this process. We investigated the response of the G. moniliformis proteome in limited nitrogen (N0, fumonisin-inducing) and excess nitrogen (N+, fumonisin-repressing) conditions by one- and two-dimensional electrophoresis. We selected 11 differentially expressed proteins, six from limited nitrogen conditions and five from excess nitrogen conditions, and determined the sequences by peptide mass fingerprinting and MS/MS spectrophotometry. Subsequently, we identified the EST sequences corresponding to the proteins and studied their expression profiles in different culture conditions. Through the comparative analysis of gene and protein expression data, we identified three candidate genes for functional analysis and our results provided valuable clues regarding the regulatory mechanisms of fumonisin biosynthesis.

The Effect of Protein Expression of Streptococcus pneumoniae by Blood

  • Bae, Song-Mee;Yeon, Sun-Mi;Kim, Tong-Soo;Lee, Kwang-Jun
    • BMB Reports
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    • v.39 no.6
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    • pp.703-708
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    • 2006
  • During infection, the common respiratory tract pathogen Streptococcus pneumoniae encounters several environmental conditions, such as upper respiratory tract, lung tissue, and blood stream, etc. In this study, we examined the effects of blood on S. pneumoniae protein expression using a combination of highly sensitive 2-dimensional electrophoresis (DE) and MALDI-TOF MS and/or LC/ESI-MS/MS. A comparison of expression profiles between the growth in THY medium and THY supplemented with blood allowed us to identify 7 spots, which increased or decreased two times or more compared with the control group: tyrosyl-tRNA synthetase, lactate oxidase, glutamyl-aminopeptidase, L-lactate dehydrogenase, cysteine synthase, ribose-phosphate pyrophosphokinase, and orotate phosphoribosyltransferase. This global approach can provide a better understanding of S. pneumoniae adaptation to its human host and a clue for its pathogenicity.

Proteomic Analysis of the Oxidative Stress Response Induced by Low-Dose Hydrogen Peroxide in Bacillus anthracis

  • Kim, Sang Hoon;Kim, Se Kye;Jung, Kyoung Hwa;Kim, Yun Ki;Hwang, Hyun Chul;Ryu, Sam Gon;Chai, Young Gyu
    • Journal of Microbiology and Biotechnology
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    • v.23 no.6
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    • pp.750-758
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    • 2013
  • Anthrax is a bacterial disease caused by the aerobic spore-forming bacterium Bacillus anthracis, which is an important pathogen owing to its ability to be used as a terror agent. B. anthracis spores can escape phagocytosis and initiate the germination process even in antimicrobial conditions, such as oxidative stress. To analyze the oxidative stress response in B. anthracis and thereby learn how to prevent antimicrobial resistance, we performed protein expression profiling of B. anthracis strain HY1 treated with 0.3 mM hydrogen peroxide using a comparative proteomics-based approach. The results showed a total of 60 differentially expressed proteins; among them, 17 showed differences in expression over time. We observed time-dependent changes in the production of metabolic and repair/protection signaling proteins. These results will be useful for uncovering the metabolic pathways and protection mechanisms of the oxidative response in B. anthracis.

Comparative Whole Cell Proteomics of Listeria monocytogenes at Different Growth Temperatures

  • Won, Soyoon;Lee, Jeongmin;Kim, Jieun;Choi, Hyungseok;Kim, Jaehan
    • Journal of Microbiology and Biotechnology
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    • v.30 no.2
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    • pp.259-270
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    • 2020
  • Listeria monocytogenes is a gram-positive, facultative anaerobe food pathogen responsible for the listeriosis that mostly occurs during the low-temperature storage of a cold cut or dairy products. To understand the systemic response to a wide range of growth temperatures, L. monocytogenes were cultivated at a different temperature from 10℃ to 42℃, then whole cell proteomic analysis has been performed both exponential and stationary cells. The specific growth rate increased proportionally with the increase in growth temperature. The maximum growth rate was observed at 37℃ and was maintained at 42℃. Global protein expression profiles mainly depended on the growth temperatures showing similar clusters between exponential and stationary phases. Expressed proteins were categorized by their belonging metabolic systems and then, evaluated the change of expression level in regard to the growth temperature and stages. DnaK, GroEL, GroES, GrpE, and CspB, which were the heat&cold shock response proteins, increased their expression with increasing the growth temperatures. In particular, GroES and CspB were expressed more than 100-fold than at low temperatures during the exponential phase. Meanwhile, CspL, another cold shock protein, overexpressed at a low temperature then exponentially decreased its expression to 65-folds. Chemotaxis protein CheV and flagella proteins were highly expressed at low temperatures and stationary phases. Housekeeping proteins maintained their expression levels constant regardless of growth temperature or growth phases. Most of the growth related proteins, which include central carbon catabolic enzymes, were highly expressed at 30℃ then decreased sharply at high growth temperatures.

Proteomic Analysis of Protein Expression in Streptococcus pneumoniae in Response to Temperature Shift

  • Lee Myoung-Ro;Bae Song-Mee;Kim Tong-Soo;Lee Kwang-Jun
    • Journal of Microbiology
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    • v.44 no.4
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    • pp.375-382
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    • 2006
  • From its initial colonization to causation of disease, Streptococcus pneumoniae has evolved strategies to cope with a number of stressful in vivo environmental conditions. In order to analyze a global view of this organism's response to heat shock, we established a 2-D electrophoresis proteome map of the S. pneumoniae D39 soluble proteins under in vitro culture conditions and performed the comparative proteome analysis to a 37 to $42^{\circ}C$ temperature up-shift in S. pneumoniae. When the temperature of an exponentially growing S. pneumoniae D39 culture was raised to $42^{\circ}C$, the expression level of 25 proteins showed changes when compared to the control. Among these 25 proteins, 12 were identified by MALDI-TOF and LC-coupled ESI MS/MS. The identified proteins were shown to be involved in the general stress response, energy metabolism, nucleotide biosynthesis pathways, and purine metabolism. These results provide clues for understanding the mechanism of adaptation to heat shock by S. pneumoniae and may facilitate the assessment of a possible role for these proteins in the physiology and pathogenesis of this pathogen.

What Can Proteomics Tell Us about Tuberculosis?

  • Susana Flores-Villalva;Elba Rogriguez-Hernandez;Yesenia Rubio-Venegas;Jorge Germinal Canto-Alarcon;Feliciano Milian-Suazo
    • Journal of Microbiology and Biotechnology
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    • v.25 no.8
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    • pp.1181-1194
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    • 2015
  • Tuberculosis (TB) is an infectious disease transmitted by aerosol droplets and characterized by forming granulomatous lesions. Although the number of people infected in the population is high, the vast majority does not exhibit symptoms of active disease and only 5-10% develop the disease after a latent period that can vary from weeks to years. The bases of the immune response for this resistance are unknown, but it depends on a complex interaction between the environment, the agent, and the host. The analysis of cellular components of M. tuberculosis shows important host-pathogen interactions, metabolic pathways, virulence mechanisms, and mechanisms of adaptation to the environment. However, the M. tuberculosis proteome still remains largely uncharacterized in terms of virulence and pathogenesis. Here, we summarize some of the major proteomic studies performed to scrutinize all the mycobacterial components.