Review
- MINIREVIEW] Rapid and robust MALDI-TOF MS techniques for microbial identification: a brief overview of their diverse applications
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Kyoung-Soon Jang , Young Hwan Kim
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J. Microbiol. 2018;56(4):209-216. Published online February 28, 2018
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DOI: https://doi.org/10.1007/s12275-018-7457-0
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Abstract
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Advances in mass spectrometry have enabled the investigation
of various biological systems by directly analyzing diverse
sets of biomolecules (i.e., proteins, lipids, and carbohydrates),
thus making a significant impact on the life sciences field.
Over the past decade, matrix-assisted laser desorption ionization
time-of-flight mass spectrometry (MALDI-TOF MS) has
been widely utilized as a rapid and reliable method for the
identification of microorganisms. MALDI-TOF MS has come
into widespread use despite its relatively low resolving power
(full width at half maximum, FWHM: < 5,000) and its incompatibility
with tandem MS analysis, features with which other
high-resolution mass spectrometers are equipped. Microbial
identification is achieved by searching databases containing
mass spectra of peptides and proteins extracted from microorganisms
of interest, using scoring algorithms to match analyzed
spectra with reference spectra. In this paper, we give
a brief overview of the diverse applications of rapid and robust
MALDI-TOF MS-based techniques for microbial identification
in a variety of fields, such as clinical diagnosis and environmental
and food monitoring. We also describe the fundamental
principles of MALDI-TOF MS. The general specifications
of the two major MS-based microbial identification
systems available in the global market (BioTyper® and VITEK®
MS Plus) and the distribution of these instruments in Republic
of Korea are also discussed. The current review provides an
understanding of this emerging microbial identification and
classification technology and will help bacteriologists and
cell biologists take advantage of this powerful technique.
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Citations
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Livia M. R. Vidal, Tainá M. Venas, Aline R. P. Gonçalves, Hannah K. Mattsson, Raphael V. P. Silva, Maria S. Nóbrega, Gustavo P. R. Azevedo, Gizele D. Garcia, Diogo A. Tschoeke, Verônica V. Vieira, Fabiano L. Thompson, Cristiane C. Thompson
Archives of Microbiology.2020; 202(8): 2329. CrossRef - Identification of pathogens from native urine samples by MALDI-TOF/TOF tandem mass spectrometry
Damir Oros, Marina Ceprnja, Jurica Zucko, Mario Cindric, Amela Hozic, Jasenka Skrlin, Karmela Barisic, Ena Melvan, Ksenija Uroic, Blazenka Kos, Antonio Starcevic
Clinical Proteomics.2020;[Epub] CrossRef - Sensitive detection of quinoline-derivatized sitagliptin in small volumes of human plasma by MALDI-TOF mass spectrometry
Yi-Shan Li, Wei-Lung Tseng, Chi-Yu Lu
Talanta.2020; 218: 121143. CrossRef - The management of anti-infective agents in intensive care units: the potential role of a ‘fast’ pharmacology
Dario Cattaneo, Alberto Corona, Francesco Giuseppe De Rosa, Cristina Gervasoni, Danijela Kocic, Deborah Je Marriott
Expert Review of Clinical Pharmacology.2020; 13(4): 355. CrossRef - Identification of bacteria in juice/lettuce using magnetic nanoparticles and selected reaction monitoring mass spectrometry
Cheng-Tung Chen, Je-Wei Yu, Yen-Peng Ho
Journal of Food and Drug Analysis.2019; 27(2): 575. CrossRef - Application of the Whole Genome-Based Bacterial Identification System, TrueBac ID, Using Clinical Isolates That Were Not Identified With Three Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS) Systems
Sung-Min Ha, Chang Ki Kim, Juhye Roh, Jung-Hyun Byun, Seung-Jo Yang, Seon-Bin Choi, Jongsik Chun, Dongeun Yong
Annals of Laboratory Medicine.2019; 39(6): 530. CrossRef - Antimicrobial random peptide cocktails: a new approach to fight pathogenic bacteria
Zaid Amso, Zvi Hayouka
Chemical Communications.2019; 55(14): 2007. CrossRef - Application of MALDI Biotyper System for Rapid Identification of Bacteria Isolated from a Fresh Produce Market
Israa Mohamad El-Nemr, Mohanad Mushtaha, Sathyavathi Sundararaju, Charmaine Fontejon, Mohammed Suleiman, Patrick Tang, Ipek Goktepe, Mohammad Rubayet Hasan
Current Microbiology.2019; 76(3): 290. CrossRef - Identification of dermatophytes by MALDI-TOF MS technology in the clinical laboratory
Maya Azrad, Victoria Freidus, Riad Kassem, Avi Peretz
International Journal of Mass Spectrometry.2019; 440: 32. CrossRef - Differences between Staphylococcus aureus lineages isolated from ovine and caprine mastitis but not between isolates from clinical or subclinical mastitis
J. Hoekstra, V.P.M.G. Rutten, M. van den Hout, M.P. Spaninks, L. Benedictus, G. Koop
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Research Support, Non-U.S. Gov't
- Comparative Proteome Analysis of Bacillus anthracis with pXO1 Plasmid Content
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Sudipto Shahid , Ji Hyun Park , Hyung Tae Lee , Seong-Joo Kim , Ji Cheon Kim , Sang Hoon Kim , Dal Mu Ri Han , Dong In Jeon , Kyoung Hwa Jung , Young Gyu Chai
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J. Microbiol. 2010;48(6):771-777. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0136-4
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Abstract
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Bacillus anthracis the causative agent of anthrax, is an important pathogen among the Bacillus cereus group of species because of its physiological characteristics and its importance as a biological warfare agent. Tripartite anthrax toxin proteins and a poly-D-glutamic acid capsule are produced by B. anthracis vegetative
cells during mammalian hosts infection and when cultured in conditions that are thought to mimic the host environment. To identify the factors regulating virulence in B. anthracis the whole cell proteins were extracted from two B. anthracis strains and separated by narrow range immobilized pH gradient (IPG) strips (pH 4-7),
followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Proteins that were differentially expressed were identified by the peptide fingerprinting using matrix-assisted laser desorption ionization–time-of-flight mass spectrometry (MALDI-TOF MS). A total of 23 proteins were identified as
being either upregulated or downregulated in the presence or absence of the virulence plasmid pXO1. Two plasmid encoded proteins and 12 cellular proteins were identified and documented as potential virulence factors.
Journal Article
- Analysis and Identification of ADP-Ribosylated Proteins of Streptomyces coelicolor M145
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András Penyige , Judit Keser , Ferenc Fazakas , Iván Schmelczer , Krisztina Szirák , György Barabás , Sándor Biró
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J. Microbiol. 2009;47(5):549-556. Published online October 24, 2009
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DOI: https://doi.org/10.1007/s12275-009-0032-y
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40
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Abstract
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Mono-ADP-ribosylation is the enzymatic transfer of ADP-ribose from NAD+ to acceptor proteins catalyzed by ADP-ribosyltransferases. Using m-aminophenylboronate affinity chromatography, 2D-gel electrophoresis, in-gel digestion and MALDI-TOF analysis we have identified eight in vitro ADP-ribosylated proteins in Streptomyces coelicolor, which can be classified into three categories: (i) secreted proteins; (ii) metabolic enzymes using NAD+/NADH or NADP+/NADPH as coenzymes; and (iii) other proteins. The secreted proteins could be classified into two functional categories: SCO2008 and SCO5477 encode members of the family
of periplasmic extracellular solute-binding proteins, and SCO6108 and SCO1968 are secreted hydrolases. Dehydrogenases are encoded by SCO4824 and SCO4771. The other targets are GlnA (glutamine synthetaseI., SCO2198) and SpaA (starvation-sensing protein encoded by SCO7629). SCO2008 protein and GlnA had been identified as ADP-ribosylated proteins in previous studies. With these results we provided experimental support for a previous suggestion that ADP-ribosylation may regulate membrane transport and localization of periplasmic proteins. Since ADP-ribosylation results in inactivation of the target protein, ADP-ribosylation of dehydrogenases might modulate crucial primary metabolic pathways in Streptomyces. Several of the proteins identified here could provide a strong connection between protein ADP-ribosylation and the regulation of morphological differentiation in S. coelicolor.
Research Support, Non-U.S. Gov't
- Comparative Proteomic Analysis of Virulent Korean Mycobacterium tuberculosis K-strain with Other Mycobacteria Strain Following Infection of U-937 Macrophage
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Sung Weon Ryoo , Young Kil Park , Sue-Nie Park , Young Soo Shim , Hyunjeong Liew , Seongman Kang , Gill-Han Bai
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J. Microbiol. 2007;45(3):268-271.
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DOI: https://doi.org/2532 [pii]
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Abstract
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In Korea, the Mycobacterium tuberculosis K-strain is the most prevalent clinical isolates and belongs to the Beijing family. In this study, we conducted comparative porteomics of expressed proteins of clinical isolates of the K-strain with H37Rv, H37Ra as well as the vaccine strain of Mycobacterium bovis BCG following phagocytosis by the human monocytic cell line U-937. Proteins were analyzed by 2-D PAGE and MALDITOF-MS. Two proteins, Mb1363 (probable glycogen phosphorylase GlgP) and MT2656 (Haloalkane dehalogenase LinB) were most abundant after phagocytosis of M. tuberculosis K-strain. This approach provides a method to determine specific proteins that may have critical roles in tuberculosis pathogenesis.