Matrix-Assisted Laser Desorption/Ionization Time-Of-Flight Mass Spectrometry In the Diagnosis of Microorganisms

Evangelista, Antonio José de Jesus; Ferreira, Thais Lima

doi:10.2217/fmb-2022-0067

Cited by 9 publications

(7 citation statements)

References 55 publications

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“…Although the suspected isolate in this exercise was phenotypically ruled out as B. anthracis , its association with the cutaneous lesion outbreak in step 1 makes it a potential source of an emerging infectious disease. MALDI-TOF is increasingly used to identify microbial pathogens in the clinical diagnostic laboratory ( 14 ). In this technique, a microbial colony is embedded within a matrix and a laser is used to ionize the sample, resulting in particles that can be separated according to their mass-to-charge ratio and measured by the time it takes for those ions to travel to a detector at the end of a time-of-flight tube.…”

Section: Methodsmentioning

confidence: 99%

A simple undergraduate laboratory exercise for teaching the role of sentinel-level clinical microbiology testing in biological threat identification

Cox,

Askew

2023

J Microbiol Biol Educ.

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Undergraduate students in the biomedical sciences are mostly unaware of how clinical microbiology laboratories handle suspected agents of bioterrorism or emerging infectious diseases. The Public Health Security Bioterrorism Preparedness and Response Act of 2002 requires the US Department of Health and Human Services (HHS) to maintain a list of microbes that pose serious biological threats to human health and safety, including Tier 1 agents with the potential for use in bioterrorism. The Laboratory Response Network (LRN), founded by the Centers for Disease Control and Prevention, the Federal Bureau of Investigation, and the Association of Public Health Laboratories, coordinates the response of sentinel, reference, and national laboratories to these biothreats. The sentinel laboratories, which comprise most hospital-based and commercial laboratories, are the first to encounter a suspicious agent. For this reason, the LRN has published a series of testing guidelines to assist the sentinel laboratories in deciding whether a microbial isolate should be considered potentially hazardous and thus sent to a reference or national laboratory for further characterization. Here, we describe a simple laboratory exercise that teaches sentinel-level testing requirements in the context of an applied setting of a potential outbreak of anthrax that would require a sentinel laboratory to recognize a potential threat, attempt to rule it out, and refer to a national laboratory for identification.

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Section: Methodsmentioning

confidence: 99%

A simple undergraduate laboratory exercise for teaching the role of sentinel-level clinical microbiology testing in biological threat identification

Cox,

Askew

2023

J Microbiol Biol Educ.

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“…Liquid chromatography and the fragmentation of peptides can be employed to determine the amino acid sequence and PTMs of interest via tandem MS analysis (MS/MS) [183][184][185] and a variety of related MS methods [186,187], including single-cell MS [188]. A ToF-based analyzer determines efficiently the mass-to-charge ratio (m/z) using the time ions require to travel through an electric field under vacuum [189]. This is combined with the MALDI-mediated detection of peptides [190].…”

Section: Mass Spectrometric Protein Identificationmentioning

confidence: 99%

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Dowling,

Swandulla,

Ohlendieck

2023

Cells

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Voluntary striated muscles are characterized by a highly complex and dynamic proteome that efficiently adapts to changed physiological demands or alters considerably during pathophysiological dysfunction. The skeletal muscle proteome has been extensively studied in relation to myogenesis, fiber type specification, muscle transitions, the effects of physical exercise, disuse atrophy, neuromuscular disorders, muscle co-morbidities and sarcopenia of old age. Since muscle tissue accounts for approximately 40% of body mass in humans, alterations in the skeletal muscle proteome have considerable influence on whole-body physiology. This review outlines the main bioanalytical avenues taken in the proteomic characterization of skeletal muscle tissues, including top-down proteomics focusing on the characterization of intact proteoforms and their post-translational modifications, bottom-up proteomics, which is a peptide-centric method concerned with the large-scale detection of proteins in complex mixtures, and subproteomics that examines the protein composition of distinct subcellular fractions. Mass spectrometric studies over the last two decades have decisively improved our general cell biological understanding of protein diversity and the heterogeneous composition of individual myofibers in skeletal muscles. This detailed proteomic knowledge can now be integrated with findings from other omics-type methodologies to establish a systems biological view of skeletal muscle function.

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“…The identification and characterization of individual proteoforms in crude tissue samples, subcellular fractions, enriched preparations of the matrisome, or isolated protein assemblies can be carried out by a variety of mass spectrometric methods [114][115][116][117], such as liquid chromatography-tandem mass spectrometry (LC-MS/MS) [115,118] or matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) [114,119]. Both labelling and label-free approaches are routinely used for the detection of protein species.…”

Section: Mass Spectrometry and Data Acquisitionmentioning

confidence: 99%

Extracellular Matrix Proteomics: The mdx-4cv Mouse Diaphragm as a Surrogate for Studying Myofibrosis in Dystrophinopathy

et al. 2023

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The progressive degeneration of the skeletal musculature in Duchenne muscular dystrophy is accompanied by reactive myofibrosis, fat substitution, and chronic inflammation. Fibrotic changes and reduced tissue elasticity correlate with the loss in motor function in this X-chromosomal disorder. Thus, although dystrophinopathies are due to primary abnormalities in the DMD gene causing the almost-complete absence of the cytoskeletal Dp427-M isoform of dystrophin in voluntary muscles, the excessive accumulation of extracellular matrix proteins presents a key histopathological hallmark of muscular dystrophy. Animal model research has been instrumental in the characterization of dystrophic muscles and has contributed to a better understanding of the complex pathogenesis of dystrophinopathies, the discovery of new disease biomarkers, and the testing of novel therapeutic strategies. In this article, we review how mass-spectrometry-based proteomics can be used to study changes in key components of the endomysium, perimysium, and epimysium, such as collagens, proteoglycans, matricellular proteins, and adhesion receptors. The mdx-4cv mouse diaphragm displays severe myofibrosis, making it an ideal model system for large-scale surveys of systematic alterations in the matrisome of dystrophic fibers. Novel biomarkers of myofibrosis can now be tested for their appropriateness in the preclinical and clinical setting as diagnostic, pharmacodynamic, prognostic, and/or therapeutic monitoring indicators.

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Matrix-Assisted Laser Desorption/Ionization Time-Of-Flight Mass Spectrometry In the Diagnosis of Microorganisms

Cited by 9 publications

References 55 publications

A simple undergraduate laboratory exercise for teaching the role of sentinel-level clinical microbiology testing in biological threat identification

A simple undergraduate laboratory exercise for teaching the role of sentinel-level clinical microbiology testing in biological threat identification

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Extracellular Matrix Proteomics: The mdx-4cv Mouse Diaphragm as a Surrogate for Studying Myofibrosis in Dystrophinopathy

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