{"product_id":"mass-spectrometry-for-microbial-proteomics-9780470681992","title":"Mass Spectrometry for Microbial Proteomics","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eNew advances in proteomics, driven largely by developments in massspectrometry, continue to reveal the complexity and diversity ofpathogenic mechanisms among microbes that underpin infectiousdiseases.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTrade Review\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e“Summary Mass Spectrometry of Microbial Proteomics provides an authoritative guide to the expanding field of microbial proteomics.”  (\u003ci\u003eAnal Bioanal Chem\u003c\/i\u003e, 2011)\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003ePreface  \u003cp\u003e List of contributors \u003cb\u003eMicrobial Characterisation; the Transition from Conventional Methods to Proteomics.\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e 1) CHANGING CONCEPTS IN THE CHARACTERISATION OF MICROBES AND THE INFLUENCE OF MASS SPECTROMETRY  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eHaroun Shah et al\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 1.1 Background and early attempts to use mass spectrometry on microbes.  \u003c\/p\u003e\u003cp\u003e 1.2 Characterisation of microorganisms by MALDI-TOF mass spectrometry; from initial ideas to the development of the first comprehensive database.  \u003c\/p\u003e\u003cp\u003e 1.3 Characterisation of microorganisms from their intracellular\/membrane bound protein profiles using affinity capture with particular reference to SELDI-TOF-MS.  \u003c\/p\u003e\u003cp\u003e 1.4 Comparative analysis of proteomes of diverse strains within a species; use of 2-d fluorescence difference gel electrophoresis (dige).  \u003c\/p\u003e\u003cp\u003e 1.5 Searching for low abundant and low molecular weight proteins and peptides using nanoparticles as a selective and concentration probes for MALDI-TOF-MS analysis.  \u003c\/p\u003e\u003cp\u003e 2) MICROBIAL PHYLOGENY AND EVOLUTION BASED ON PROTEIN SEQUENCES (THE CHANGE FROM TARGETED GENES TO PROTEINS)  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eRadhey Gupta\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 2.1 Abstract  \u003c\/p\u003e\u003cp\u003e 2.2 Microbial phylogeny: overview and key unresolved issues  \u003c\/p\u003e\u003cp\u003e 2.3 New protein-based molecular markers for systematic and evolutionary studies  \u003c\/p\u003e\u003cp\u003e 2.4 Molecular markers elucidating the evolutionary relationships among alpha (a)-proteobacteria  \u003c\/p\u003e\u003cp\u003e 2.5 Molecular markers for the bacteroidetes-chlorobi phyla  \u003c\/p\u003e\u003cp\u003e 2.6 Branching order and interrelationships among bacterial phyla  \u003c\/p\u003e\u003cp\u003e 2.7 Importance of protein markers for discovering unique properties for different groups of bacteria  \u003c\/p\u003e\u003cp\u003e 2.8 Concluding remarks  \u003c\/p\u003e\u003cp\u003e 2.9 Acknowledgements  \u003c\/p\u003e\u003cp\u003e 2.10 References  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e2: PROTEOMICS TOOLS AND BIOMARKER DISCOVERY.\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e 3) OVERVIEW OF THE PROTEOMIC TOOLS AND IT LINKS TO GENOMICS  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eRaju Misra.\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 3.1 Protein identification  \u003c\/p\u003e\u003cp\u003e 3.2 Peptide Mass Fingerprint (PMF)  \u003c\/p\u003e\u003cp\u003e 3.3 Peptide Fragment Fingerprint (PFF)  \u003c\/p\u003e\u003cp\u003e 3.4 Peptide sequencing  \u003c\/p\u003e\u003cp\u003e 3.5 False discovery rates (FDR)  \u003c\/p\u003e\u003cp\u003e 3.6 Validating protein identifications  \u003c\/p\u003e\u003cp\u003e 3.7 Reference Database  \u003c\/p\u003e\u003cp\u003e 3.8 Data storage  \u003c\/p\u003e\u003cp\u003e 3.9 Biomarker discovery  \u003c\/p\u003e\u003cp\u003e 3.10 Integrating genomics with proteomics  \u003c\/p\u003e\u003cp\u003e 3.11 Reference List  \u003c\/p\u003e\u003cp\u003e 4) HIGH THROUGHPUT BIOMARKER DISCOVERY IN MICROORGANISMS  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eMing Fang\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 4.1 MALDI vs ESI  \u003c\/p\u003e\u003cp\u003e 4.2 Tandem Mass Spectrometry and Hybrid Mass Spectrometers  \u003c\/p\u003e\u003cp\u003e 4.3 Fragmentation in Tandem Mass Spectrometry  \u003c\/p\u003e\u003cp\u003e Proteomic Strategies for Protein Identification  \u003c\/p\u003e\u003cp\u003e 1. Bottom-up Proteomics  \u003c\/p\u003e\u003cp\u003e 2. Top-down Proteomics  \u003c\/p\u003e\u003cp\u003e Multidimensional Protein Identification  \u003c\/p\u003e\u003cp\u003e Mass Spectrometry Based Targeted Protein Quantification and Biomarker Discovery  \u003c\/p\u003e\u003cp\u003e Selected Reaction Monitoring  \u003c\/p\u003e\u003cp\u003e Conclusions  \u003c\/p\u003e\u003cp\u003e 5) MALDI MASS SPECTROMETRY IMAGING, A NEW FRONTIER IN BIOSTRUCTURAL TECHNIQUES: APPLICATIONS IN BIOMEDICINE \u003ci\u003eSimona Francese and Malcolm R. Clench\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 5.1 Introduction  \u003c\/p\u003e\u003cp\u003e 5.2 Practical Aspects of MALDI-MSI  \u003c\/p\u003e\u003cp\u003e 5.2 Applications  \u003c\/p\u003e\u003cp\u003e 5.3 Microbial molecular investigation by MALDI TOF MS  \u003c\/p\u003e\u003cp\u003e 5.4 Conclusions  \u003c\/p\u003e\u003cp\u003e 5.5 References  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e3: PROTEIN SAMPLES PREPARATION TECHNIQUES\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e CONVENTIONAL APPROACHES FOR SAMPLE PREPARATION FOR LIQUID  \u003c\/p\u003e\u003cp\u003e CHROMATOGRAPHY AND TWO-DIMENSIONAL GEL ELECTROPHORESIS  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eVesela Encheva and Robert Parker\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 6.1 Introduction  \u003c\/p\u003e\u003cp\u003e 6.2 Cell lysis methods  \u003c\/p\u003e\u003cp\u003e 6.3 Sample preparation for 2D GE  \u003c\/p\u003e\u003cp\u003e 6.4 Fractionation strategies  \u003c\/p\u003e\u003cp\u003e 6.5 Sample preparation for Liquid Chromatography coupled to mass  \u003c\/p\u003e\u003cp\u003e 6.6 Conclusion  \u003c\/p\u003e\u003cp\u003e 6.7 Reference list  \u003c\/p\u003e\u003cp\u003e 7) ISOLATION AND PREPARATION OF SPORE PROTEINS AND SUBSEQUENT CHARACTERISATION BY ELECTROPHORESIS AND MASS SPECTROMETRY \u003ci\u003eNicola Thorne, Saheer Gharbia and Haroun Shah\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 7.1 Introduction  \u003c\/p\u003e\u003cp\u003e 7.2 Experimental  \u003c\/p\u003e\u003cp\u003e \u003ci\u003e2.1 Sporulation media\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 7.3 Conclusion  \u003c\/p\u003e\u003cp\u003e 8) CHARACTERIZATION OF BACTERIAL MEMBRANE PROTEINS USING A NOVEL COMBINATION OF A LIPID BASED PROTEIN IMMOBILIZATION TECHNIQUE WITH MASS SPECTROMETRY  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eRoger Karlsson, Darren Chooneea, Elisabet Carlsohn, Vesela Encheva and Haroun Shah\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 8.1 Introduction  \u003c\/p\u003e\u003cp\u003e 8.2 The surface proteome  \u003c\/p\u003e\u003cp\u003e 8.3 Proteomics of pathogenic bacteria  \u003c\/p\u003e\u003cp\u003e 8.4 Lipid-based protein immobilization technology  \u003c\/p\u003e\u003cp\u003e 8.5 Salmonella Typhimurium – disease mechanism and outer membrane proteins  \u003c\/p\u003e\u003cp\u003e 8.6 Outer membrane proteins of S. Typhimurium  \u003c\/p\u003e\u003cp\u003e 8.7 Helicobacter pylori – disease mechanism and outer membrane proteins  \u003c\/p\u003e\u003cp\u003e 8.8 Surface proteins of intact Helicobacter pylori  \u003c\/p\u003e\u003cp\u003e 9) Wider Protein Detection from Biological Extracts by the Reduction of Dynamic Concentration Range.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eLuc Guerrier, Egisto Boschetti and Piergiorgi Roghetti\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 9.1 Introduction  \u003c\/p\u003e\u003cp\u003e 9.2 Dealing with low-abundance protein discovery  \u003c\/p\u003e\u003cp\u003e 9.3 Conclusions and future prospects  \u003c\/p\u003e\u003cp\u003e 9.4 References  \u003c\/p\u003e\u003cp\u003e 10) 3D-gel electrophoresis - a new development in protein analysis.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eRobert Ventzki and Josef Stegemann\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 10.1. Introduction  \u003c\/p\u003e\u003cp\u003e 10.2. Methods  \u003c\/p\u003e\u003cp\u003e 10.3 Results and discussion  \u003c\/p\u003e\u003cp\u003e 10.4 References  \u003c\/p\u003e\u003cp\u003e \u003cb\u003eSECTION 4: CHARACTERISATION OF MICROORGANISMS BY PATTERN MATCHING OF MASS SPECTRAL PROFILES AND BIOMARKER APPROACHES REQUIRING MINIMAL SAMPLE PREPARATION.\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e 11) Microbial Disease Biomarkers using ProteinChip Arrays  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eShea Hamilton, Michael Levin, J. Simon Kroll, Paul R. Langford\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 11.1 Introduction  \u003c\/p\u003e\u003cp\u003e 11.2 Biomarker studies involving patients infected with viruses  \u003c\/p\u003e\u003cp\u003e 11.3 Biomarker studies involving patients infected with parasites  \u003c\/p\u003e\u003cp\u003e 11.4 Biomarker studies involving patients infected with bacteria  \u003c\/p\u003e\u003cp\u003e 11.5 Other diseases of possible infectious origin  \u003c\/p\u003e\u003cp\u003e 11.6 Conclusions  \u003c\/p\u003e\u003cp\u003e 11.7 References  \u003c\/p\u003e\u003cp\u003e 12) MALDI-TOF MS and microbial identification: years of experimental  \u003c\/p\u003e\u003cp\u003e development to an established protocol.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eWibke Kallow, Marcel Erhard,\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eHaroun N. Shah, Emmanuel Raptakis, Martin Welker.\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 12.1 Identification of Microorganisms in Clinical Routine  \u003c\/p\u003e\u003cp\u003e 12.2 Mass Spectrometry and Microbiology  \u003c\/p\u003e\u003cp\u003e 12.3 Mass Spectral ‘Fingerprints’ of Whole Cells  \u003c\/p\u003e\u003cp\u003e 12.4 Reproducibility of Mass Spectral Fingerprints  \u003c\/p\u003e\u003cp\u003e 12.5 Species and Strain Discrimination by Mass Spectrometry  \u003c\/p\u003e\u003cp\u003e 12.6 Pattern Matching Approaches for automated Identification  \u003c\/p\u003e\u003cp\u003e 12.7 Mass Spectral Identification of Microorganism – Requirements for Routine Diagnostics  \u003c\/p\u003e\u003cp\u003e 12.8 Automated Mass Spectral Analysis of Microorganisms in Clinical Routine Diagnostics  \u003c\/p\u003e\u003cp\u003e 12.9 Acknowledgements and references  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e5: Targeted Molecules and Analysis of Specific Microorganisms.\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e 13) Whole Cell MALDI Mass Spectrometry for the Rapid Characterisation of  \u003c\/p\u003e\u003cp\u003e Bacteria; A Survey of Applications to Major Phyletic Lines in Microbial  \u003c\/p\u003e\u003cp\u003e Kingdom.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eBen van Baar\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 13.1 Introduction  \u003c\/p\u003e\u003cp\u003e 13.2Scope  \u003c\/p\u003e\u003cp\u003e 13.3 Reproducibility  \u003c\/p\u003e\u003cp\u003e 13.3.1 \u003ci\u003eFactors concerning the sample\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 13.4 Factors concerning the MALDI MS process  \u003c\/p\u003e\u003cp\u003e 13.5 Sample application and ionisation  \u003c\/p\u003e\u003cp\u003e 13.5 Data analysis  \u003c\/p\u003e\u003cp\u003e 13.6 Spectrum libraries  \u003c\/p\u003e\u003cp\u003e 13.6Whole cell MALDI MS of particular bacteria genera and species  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eBacillus\u003c\/i\u003e spp\u003ci\u003e.\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eStaphylococcus\u003c\/i\u003e spp.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eStreptococcus\u003c\/i\u003e spp.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eMycobacterium\u003c\/i\u003e spp.  \u003c\/p\u003e\u003cp\u003e Other Gram-positive bacteria  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eEscherichia coli\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Gram-negative food- and waterborne pathogen proteobacteria, other than E. Coli  \u003c\/p\u003e\u003cp\u003e Typical sexually transmitted pathogens: Neisseria \u003ci\u003espp. and\u003c\/i\u003e Haemophilus \u003ci\u003espp.\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Gram-negative biothreat agent bacteria  \u003c\/p\u003e\u003cp\u003e Other Gram-negative bacteria  \u003c\/p\u003e\u003cp\u003e \u003ci\u003ePathogenic Cyanobacteria\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Strategies for the identification of biomarkers in whole cell MALDI MS spectra  \u003c\/p\u003e\u003cp\u003e Protein database consideration  \u003c\/p\u003e\u003cp\u003e On-target treatment and analysis  \u003c\/p\u003e\u003cp\u003e Off-target’ Analysis and correlation with proteomics studies  \u003c\/p\u003e\u003cp\u003e General consideration of biomarker identification strategies  \u003c\/p\u003e\u003cp\u003e Conclusions and outlook  \u003c\/p\u003e\u003cp\u003e 14) The power of Gel-based proteomics to understand  \u003c\/p\u003e\u003cp\u003e physiology in \u003ci\u003eBacillus subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eHaike Antelmann and Michael Hecker\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Introduction  \u003c\/p\u003e\u003cp\u003e Results  \u003c\/p\u003e\u003cp\u003e 1 Proteomics of protein secretion mechanisms in \u003ci\u003eBacillus subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 1.1. Protein export machineries of \u003ci\u003eB. subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 1.1 The extracellular proteome of \u003ci\u003eB. subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 1.2 The cell wall proteome of \u003ci\u003eB. subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 1.3. The membrane attached lipoproteome of \u003ci\u003eB. subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 1.3 The proteome analysis of protein secretion mechanisms in \u003ci\u003eB. subtilis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 2 Definition of proteomic signatures to study cell physiology  \u003c\/p\u003e\u003cp\u003e 2.1. Proteomic signatures of \u003ci\u003eB. subtilis\u003c\/i\u003e in response to stress and starvation  \u003c\/p\u003e\u003cp\u003e 2.2. Proteomic signatures of \u003ci\u003eB. subtilis\u003c\/i\u003e in response to thiol-reactive electrophiles uncovered novel regulatory mechanisms  \u003c\/p\u003e\u003cp\u003e 2.3. The MarR\/DUF24-family YodB repressor is directly sensing thiol- reactive electrophiles \u003ci\u003evia\u003c\/i\u003e the conserved Cys6 residue  \u003c\/p\u003e\u003cp\u003e 3 Proteomics as tool to visualize reversible and irreversible thiol- modifications  \u003c\/p\u003e\u003cp\u003e 3.1. The thiol-redox proteome of \u003ci\u003eB. subtilis\u003c\/i\u003e in response to diamide and quinones  \u003c\/p\u003e\u003cp\u003e 3.2. Depletion of thiol-containing proteins by quinones due to thiol-(S)- alkylation  \u003c\/p\u003e\u003cp\u003e 4 Proteomics as tool to define regulon structures and targets for non- coding RNAs  \u003c\/p\u003e\u003cp\u003e 5 Acknowledgment  \u003c\/p\u003e\u003cp\u003e 15) Mass Spectrometry in the study of Tularemia Pathogenesis.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eJiri Stulik, Juraj Lenco, Jiri Dresler, Jana Klimentova, Lenka Hernychova, Lucie Balonova and Alena Fucikova.\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e \u003ci\u003e15.1\u003c\/i\u003e Introduction to molecular pathogenesis of \u003ci\u003eFrancisella tularensis\u003c\/i\u003e infection  \u003c\/p\u003e\u003cp\u003e \u003ci\u003e15.2 Francisella tularensis\u003c\/i\u003e LVS proteome alterations induced by different temperatures and stationary phase of growth  \u003c\/p\u003e\u003cp\u003e 15.3Analysis of membrane protein complexes of \u003ci\u003eFrancisella tularensis\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 15.4 Analysis of \u003ci\u003eFrancisella tularensis\u003c\/i\u003e glycoproteins and phosphoproteins  \u003c\/p\u003e\u003cp\u003e 15.5Identification of \u003ci\u003eFrancisella tularensis\u003c\/i\u003e transcription factors potentially involved in its virulence  \u003c\/p\u003e\u003cp\u003e 15.6 Acknowledgements  \u003c\/p\u003e\u003cp\u003e References  \u003c\/p\u003e\u003cp\u003e 16) Bacterial Post-Genomics for Vaccine development  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eGiulia Bernardini, Daniela Braconi and Annalisa Santucci\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Summary  \u003c\/p\u003e\u003cp\u003e comparative genomics  \u003c\/p\u003e\u003cp\u003e transcriptomics  \u003c\/p\u003e\u003cp\u003e proteomics and immmunoproteomics  \u003c\/p\u003e\u003cp\u003e other high-throughput technologies  \u003c\/p\u003e\u003cp\u003e meningococcal vaccines and reverse vaccinology  \u003c\/p\u003e\u003cp\u003e \u003ci\u003ehelicobacter pylori\u003c\/i\u003e vaccines  \u003c\/p\u003e\u003cp\u003e conclusions  \u003c\/p\u003e\u003cp\u003e references  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e6 Statistical Analysis of 2D Gels and Analysis of Mass Spectral Data\u003c\/b\u003e  \u003c\/p\u003e\u003col\u003e\u003cli\u003eMachine Learning Techniques for the Analysis of Mass spectrometry Data. \u003c\/li\u003e\u003c\/ol\u003e  \u003cp\u003e \u003ci\u003eGraham Ball and Ali Al-Shahib\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 17.1 Introduction  \u003c\/p\u003e\u003cp\u003e 17.2 Pre-processing MS data  \u003c\/p\u003e\u003cp\u003e 17.3 Classification of MS data  \u003c\/p\u003e\u003cp\u003e 17.4 Evaluation of Classification Models  \u003c\/p\u003e\u003cp\u003e 18) Mass Spectrometry for microbial Proteomics: Issues in data analysis with  \u003c\/p\u003e\u003cp\u003e electrophoretic or mass spectrometric expression proteomic data.  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eNatasha A. Karp\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Title page  \u003c\/p\u003e\u003cp\u003e Foreword  \u003c\/p\u003e\u003cp\u003e 18.1 Introduction  \u003c\/p\u003e\u003cp\u003e 18.2 Experimental design  \u003c\/p\u003e\u003cp\u003e 18.3 Data analysis  \u003c\/p\u003e\u003cp\u003e 18.4 Validation  \u003c\/p\u003e\u003cp\u003e 18.5 Conclusions  \u003c\/p\u003e\u003cp\u003e 18.6 Figure legends  \u003c\/p\u003e\u003cp\u003e 18.7 References  \u003c\/p\u003e\u003cp\u003e \u003cb\u003eSection 7: DNA Resequencing by MALDI-TOF-Mass Spectrometry and its\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e \u003cb\u003eApplication to Traditional Microbiological Problems.\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e (19) Comparative DNA sequence analysis and typing using Mass  \u003c\/p\u003e\u003cp\u003e Spectrometry  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eChristiane Honisch,Yong Chen and Franz Hillenkamp\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e 19.1 Introduction  \u003c\/p\u003e\u003cp\u003e 19.2 Comparative Sequence Analysis by MALDI-TOF MS  \u003c\/p\u003e\u003cp\u003e 19.3 Applications of nucleic acid analysis by MALDI-TOF MS in clinical microbiology  \u003c\/p\u003e\u003cp\u003e 19.4 Conclusion  \u003c\/p\u003e\u003cp\u003e References  \u003c\/p\u003e\u003cp\u003e (20) Transfer of a Traditional Serotyping System (Kauffmann-White)  \u003c\/p\u003e\u003cp\u003e onto a MALDI-TOF-MS platform for the rapid Typing of \u003ci\u003eSalmonella\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e isolates\u003ci\u003e.\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eChloe Bishop, Cath Arnold and Saheer Gharbia\u003c\/i\u003e  \u003c\/p\u003e\u003cp\u003e Typing of salmonella isolates  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e1.1 Introduction\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e1.2 Salmonella, the pathogen\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e Biology  \u003c\/p\u003e\u003cp\u003e Pathogenesis  \u003c\/p\u003e\u003cp\u003e Clinical Disease  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e1.3 Complex genetic structure and the need to subtype this genus\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e Phylogeny  \u003c\/p\u003e\u003cp\u003e Virulence and Gene Transfer  \u003c\/p\u003e\u003cp\u003e Necessity to subtype  \u003c\/p\u003e\u003cp\u003e \u0026gt;\u003cb\u003e1.4 Antigenic Analysis - The Traditional Kauffmann - White Schema and its future\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e Serotyping  \u003c\/p\u003e\u003cp\u003e Flagellar Antigens  \u003c\/p\u003e\u003cp\u003e Flagellar Variation  \u003c\/p\u003e\u003cp\u003e Somatic Antigens  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e1.5 Sequence-based methods to determine serotypes\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e Flagellin sequences correspond directly to Salmonella serotype.  \u003c\/p\u003e\u003cp\u003e Specific SNPs  \u003c\/p\u003e\u003cp\u003e Subtyping by antigen sequence  \u003c\/p\u003e\u003cp\u003e Variation of the \u003ci\u003eRfb\u003c\/i\u003e Genes  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e1.6 Transferring the Sequences to a MALDI platform for Rapid Analysis\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e Intro  \u003c\/p\u003e\u003cp\u003e Different methods available  \u003c\/p\u003e\u003cp\u003e MALDI-TOF data analysis  \u003c\/p\u003e\u003cp\u003e \u003ci\u003eSalmonella\u003c\/i\u003e molecular serotyping as a Case Study  \u003c\/p\u003e\u003cp\u003e Gene Selection  \u003c\/p\u003e\u003cp\u003e Results Overview  \u003c\/p\u003e\u003cp\u003e Clustering and Sequence Variation of Amplicons  \u003c\/p\u003e\u003cp\u003e \u003cb\u003e1.7 Conclusions and Summary\u003c\/b\u003e  \u003c\/p\u003e\u003cp\u003e Closing Remarks\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49402407518551,"sku":"9780470681992","price":89.25,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9780470681992.jpg?v=1730480307","url":"https:\/\/bookcurl.com\/products\/mass-spectrometry-for-microbial-proteomics-9780470681992","provider":"Book Curl","version":"1.0","type":"link"}