scholarly journals Applications of MALDI Mass Spectrometry in Clinical Chemistry

2016 ◽  
Vol 62 (1) ◽  
pp. 134-143 ◽  
Author(s):  
Mark W Duncan ◽  
Dobrin Nedelkov ◽  
Ryan Walsh ◽  
Stephen J Hattan
Keyword(s):  
Mass Spectrometry ◽  
Clinical Chemistry ◽  
Cost Effective ◽  
Maldi Mass Spectrometry ◽  
Ease Of Use ◽  
Mass Detection ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

Abstract BACKGROUND MALDI-TOF mass spectrometry (MS) is set to make inroads into clinical chemistry because it offers advantages over other analytical platforms. These advantages include low acquisition and operating costs, ease of use, ruggedness, and high throughput. When coupled with innovative front-end strategies and applied to important clinical problems, it can deliver rapid, sensitive, and cost-effective assays. CONTENT This review describes the general principles of MALDI-TOF MS, highlights the unique features of the platform, and discusses some practical methods based upon it. There is substantial potential for MALDI-TOF MS to make further inroads into clinical chemistry because of the selectivity of mass detection and its ability to independently quantify proteoforms. SUMMARY MALDI-TOF MS has already transformed the practice of clinical microbiology and this review illustrates how and why it is now set to play an increasingly important role in in vitro diagnostics in particular, and clinical chemistry in general.

Chemoselective ligation reaction of N-acetylglucosamine (NAG) with hydrazide functional probes to determine galactosyltransferase activity by MALDI mass spectrometry

The Analyst ◽  
2017 ◽  
Vol 142 (14) ◽  
pp. 2654-2662 ◽  
Author(s):  
Hyojik Yang ◽  
Quan Cheng
Keyword(s):  
Mass Spectrometry ◽  
Enzymatic Activity ◽  
Gold Surface ◽  
Maldi Mass Spectrometry ◽  
Chemoselective Ligation ◽  
Maldi Tof Ms ◽  
Ligation Reaction ◽  
Maldi Tof ◽  
Tof Ms

A perfluorocarbon-modified gold surface is used to immobilize PF-β-NAG and allows quantification of β-GT enzymatic activity with MALDI-TOF/MS.

scholarly journals Rapid and cost-effective identification of Bartonella species using mass spectrometry

2009 ◽  
Vol 58 (9) ◽  
pp. 1154-1159 ◽  
Author(s):  
Pierre-Edouard Fournier ◽  
Carine Couderc ◽  
Sylvain Buffet ◽  
Christophe Flaudrops ◽  
Didier Raoult
Keyword(s):  
Mass Spectrometry ◽  
Species Identification ◽  
Chemical Reactivity ◽  
Bacterial Species ◽  
Cost Effective ◽  
Molecular Techniques ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Flight Mass Spectrometry ◽  
Tof Ms

Bacteria of the genus Bartonella are emerging zoonotic bacteria recognized in a variety of human diseases. Due to their poor chemical reactivity, these fastidious bacteria are poorly characterized using routine phenotypic laboratory tests. Identification is usually achieved using molecular techniques that are time-consuming, expensive and technically demanding. Recently, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has emerged as a new technique for bacterial species identification. This study evaluated the use of MALDI-TOF MS for rapid genus and species identification of Bartonella species. Reference strains representing 17 recognized Bartonella species were studied. For each species, MS spectra for four colonies were analysed. The consensus spectrum obtained for each species was unique among spectra obtained for 2843 bacteria within the Bruker database, including 109 alphaproteobacteria. Thirty-nine additional blind-coded Bartonella strains were correctly identified at the species level, including 36 with a significant score. Altogether, these data demonstrate that MS is an accurate and reproducible tool for rapid and inexpensive identification of Bartonella species.

scholarly journals Detection of Colistin Resistance in Escherichia coli by Use of the MALDI Biotyper Sirius Mass Spectrometry System

2019 ◽  
Vol 57 (12) ◽  
Author(s):  
R. Christopher D. Furniss ◽  
Laurent Dortet ◽  
William Bolland ◽  
Oliver Drews ◽  
Katrin Sparbier ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Escherichia Coli ◽  
Cost Effective ◽  
Colistin Resistance ◽  
Content Type ◽  
Maldi Tof Ms ◽  
E Coli ◽  
Maldi Tof ◽  
Maldi Biotyper ◽  
Tof Ms

ABSTRACT Polymyxin antibiotics are a last-line treatment for multidrug-resistant Gram-negative bacteria. However, the emergence of colistin resistance, including the spread of mobile mcr genes, necessitates the development of improved diagnostics for the detection of colistin-resistant organisms in hospital settings. The recently developed MALDIxin test enables detection of colistin resistance by matrix-assisted laser desorption ionization–time of flight mass spectrometry (MALDI-TOF MS) in less than 15 min but is not optimized for the mass spectrometers commonly found in clinical microbiology laboratories. In this study, we adapted the MALDIxin test for the MALDI Biotyper Sirius MALDI-TOF MS system (Bruker Daltonics). We optimized the sample preparation protocol by using a set of 6 mobile colistin resistance (MCR) protein-expressing Escherichia coli clones and validated the assay with a collection of 40 E. coli clinical isolates, including 19 confirmed MCR protein producers, 12 colistin-resistant isolates that tested negative for commonly encountered mcr genes (i.e., likely chromosomally resistant isolates), and 9 polymyxin-susceptible isolates. We calculated polymyxin resistance ratio (PRR) values from the acquired spectra; PRR values of 0, indicating polymyxin susceptibility, were obtained for all colistin-susceptible E. coli isolates, whereas positive PRR values, indicating resistance to polymyxins, were obtained for all resistant strains, independent of the genetic basis of resistance. Thus, we report a preliminary feasibility study showing that an optimized version of the MALDIxin test adapted for the routine MALDI Biotyper Sirius system provides an unbiased, fast, reliable, cost-effective, and high-throughput way of detecting colistin resistance in clinical E. coli isolates.

scholarly journals Human Neutrophil Peptides 1–3 as Gastric Cancer Tissue Markers Measured by MALDI-Imaging Mass Spectrometry: Implications for Infiltrated Neutrophils as a Tumor Target

2012 ◽  
Vol 32 (1) ◽  
pp. 21-31 ◽  
Author(s):  
Chun-Chia Cheng ◽  
Jungshan Chang ◽  
Ling-Yun Chen ◽  
Ai-Sheng Ho ◽  
Ker-Jer Huang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gastric Cancer ◽  
Human Neutrophil ◽  
Binding Capacity ◽  
Tumor Target ◽  
Ags Cells ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

Objective: Human neutrophil peptides (HNPs) -1, -2 and -3 are significantly upregulated and were reported as biomarkers in gastric cancer (GC). However, the tissue location and function of HNPs 1-3 are still unclear in GC, and the spatial distribution of the triad needs to be disclosed. The aims of this study were to investigate the distribution and relationships among HNPs-1, -2 and -3, and assess whether infiltrated neutrophils accumulate in gastric tumor.Methods: In this study, paired samples (n=33) of the GC tissues and adjacent normal tissues from the same patients were obtained from surgery. Expression of HNPs 1-3 were detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). The distributions of the HNPs 1-3 in GC tissues were investigated. After verification of HNPs-1 by immunohistochemistry, infiltrated neutrophils were also detected. Then, an in vitro assay was used to observe the binding capacity and measure the cytotoxic effect of HNPs-1 against AGS cells.Results: Comparing to neighboring normal tissue, expressional level of HNPs 1-3 were significantly higher and their distributions overlapped in cancerous tissues of GC patients with high abundance in the lamina propria, whereas HNPs-1 was identified as the highest major peak. Moreover, HNPs-1, -2 and -3 correlated with each other. Besides, we also observed that increased infiltrated neutrophils accumulating in GC tissues, indicating that a strong positive correlation between HNPs 1-3 and infiltrated neutrophils. In addition, the further investigated demonstrated that the major peptide, HNPs-1, was statistically increased with the advance of tumor development from the early to advanced stage of GC (p < 0.05). Moreover, we also noticed that HNPs-1 with a great binding capacity to GC AGS cells in vitro can inhibit tumor cell growth.Conclusions: Our results suggest that neutrophil secreted peptides, HNPs 1-3, increased in the GC tissues and could be used as potential biomarkers detected using MALDI-TOF MS, implying that elevated neutrophils may be used as a tumor target for tumor treatment. The binding capacity of HNPs-1 with GC cells implies that tracking molecules conjugated with HNPs-1 could be applied as a specific probe for GC diagnoses.

Rapid Identification of Commercial Frankincense Products by MALDI-TOF Mass Spectrometry

2021 ◽  
Vol 24 ◽  
Author(s):  
Shang-Chih Lai ◽  
Ren-In You ◽  
Tz-Ting Chen ◽  
Yu Chang ◽  
Chao-Zong Liu ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Throughput ◽  
High Throughput Screening ◽  
Large Scale ◽  
Reference Sample ◽  
Maldi Tof Ms ◽  
Boswellic Acids ◽  
Maldi Tof ◽  
Tof Ms

Background: Frankincense is a resin secreted by the Boswellia tree. It is used in perfumery, aromatherapy, skincare, and traditional Chinese medicine. However, all Boswellia species are under threat owing to habitat loss and overexploitation. As a result, the market is getting flooded with counterfeit frankincense products. Objective: This study aims to establish a high-throughput method to screen and identify the authenticity of commercial frankincense products. We report, for the first time, a matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS)-based method for rapid and high-throughput screening of frankincense samples. Methods: MALDI-TOF MS, HPLC, thin-layer chromatography (TLC), and in vitro anti-inflammatory activity assay were used to examine the frankincense samples. Results: Well-resolved peaks of frankincense triterpenoids in the spectra were observed in the crude extract of commercial samples, including α-boswellic acids (αBAs), β-boswellic acids (βBAs), 11-keto-β-boswellic acids (KBAs), acetyl-11-keto-β-boswellic acids (AKBAs), and their esters. These compounds can be used as indicators for determining the authenticity of frankincense. Conclusion: Unlike LC–MS, which is a time-consuming and expensive method, and TLC, which requires a reference sample, our inexpensive, rapid high-throughput identification method based on MALDI-TOF MS is ideal for large-scale screening of frankincense samples sold in the market.

scholarly journals Diagnostic accuracy of MALDI-TOF mass spectrometry for the direct identification of clinical pathogens from urine

Open Medicine ◽  
2020 ◽  
Vol 15 (1) ◽  
pp. 266-273
Author(s):  
Min Tang ◽  
Jia Yang ◽  
Ying Li ◽  
Luhua Zhang ◽  
Ying Peng ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Likelihood Ratio ◽  
Meta Analysis ◽  
Positive Likelihood Ratio ◽  
Negative Likelihood Ratio ◽  
Urine Samples ◽  
Direct Identification ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

AbstractMatrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF MS) has become one of the most popular methods for the rapid and cost-effective detection of clinical pathogenic microorganisms. This study aimed to evaluate and compare the diagnostic performance of MALDI-TOF MS with that of conventional approaches for the direct identification of pathogens from urine samples. A systematic review was conducted based on a literature search of relevant databases. The pooled sensitivity, specificity, positive likelihood ratio (PLR), negative likelihood ratio (NLR) and area under the summary receiver operating characteristic (SROC) curve of the combined studies were estimated. Nine studies with a total of 3920 subjects were considered eligible and included in the meta-analysis. The pooled sensitivity was 0.85 (95% CI 0.79-0.90), and the pooled specificity was 0.93 (95% CI 0.82-0.97). The PLR and NLR were 11.51 (95% CI 4.53-29.26) and 0.16 (95% CI 0.11-0.24), respectively. The area under the SROC curve was 0.93 (95% CI 0.91-0.95). Sensitivity analysis showed that the results of this meta-analysis were stable. MALDI-TOF MS could directly identify microorganisms from urine samples with high sensitivity and specificity.

scholarly journals The Use of MALDI-TOF Mass Spectrometry to Analyze Commensal Oral Yeasts in Nursing Home Residents

2021 ◽  
Vol 9 (1) ◽  
pp. 142
Author(s):  
Jang-Jih Lu ◽  
Hsiu-Jung Lo ◽  
Chih-Hua Lee ◽  
Mei-Jun Chen ◽  
Chih-Chao Lin ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Nursing Home ◽  
Dna Sequences ◽  
Nursing Home Residents ◽  
Practical Method ◽  
Elderly Subjects ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Oral Yeasts ◽  
Tof Ms

Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) is a rapid and accurate method to identify microorganisms in clinical laboratories. This study isolates yeast-like microorganisms in the oral washes that are collected from non-bedridden nursing home residents, using CHROMagar Candida plates, and identifies them using Bruker MALDI-TOF MS. The ribosomal DNA sequences of the isolates are then examined. Three hundred and twenty yeast isolates are isolated from the oral washes. Candida species form the majority (78.1%), followed by Trichosporon/Cutaneotrichosporon species (8.8%). Bruker MALDI-TOF MS gives a high-level confidence, with a log(score) value of ≥1.8, and identifies 96.9% of the isolates. There are six inconclusive results (1.9%), and those sequences are verified as rare clinical species, including Candida ethanolica, Cutaneotrichosporon jirovecii, Exophiala dermatitidis, and Fereydounia khargensis. Almost all of the isolates have a regular color on the CHROMagar Candida plates. If the colonies are grouped by color on the plates, a specific dominant yeast species is present in each color group, except for purple or orange isolates. In conclusion, MALDI-TOF MS is verified as a fast, accurate and practical method to analyze oral yeasts in elderly subjects.

Microorganism idenitfication – stability and correctness of mass spectrometry method (MALDI TOF MS)

2021 ◽  
Vol 56 (4) ◽  
pp. 1-12
Author(s):  
Łukasz Hildebrant ◽  
Urszula Wendt
Keyword(s):  
Mass Spectrometry ◽  
Quality Control ◽  
Control System ◽  
High Stability ◽  
Spectrometry Method ◽  
Maldi Tof Ms ◽  
Mass Spectrometry Method ◽  
Maldi Tof ◽  
Reference Strains ◽  
Tof Ms

Introduction: MALDI TOF MS method is increasingly used in routine microbiological diagnostics to identify clinical strains. The result of the identification test is based on the measurement of the mass, charge and flight time of the protein ions. This makes it possible to monitor and supervise the method using a numerical score developed with statistical techniques. Aim: The study aimed to determine the stability and correctness of the mass spectrometry method. Materials and methods: To evaluate the characteristics of the method, microbial identification tests were performed using reference strains. All tests were performed as part of the MALDI TOF MS internal quality control system. Results: All reference strains (100%) were correctly identified to the species level, although the score values were not always within the reliability criteria of the results established by the producer. It was found that the mean values of the score were from 2.000 – 2.299 (49.2%) and 2.300 – 3.000 (50.0%). The coefficient of variation for control tests performed in the consecutive years ranged from 5.18 – 6.56%, which evidence of the high stability of the method. For individual species, reproducibility precision over the 8 years ranged from 2.89% (n = 13) for Enterococcus faecalis ATCC 51299 to 7.02% (n = 28) for Klebsiella pneumoniae ATCC 700603, which proves the high precision of measurements. Conclusions: The mass spectrometry method is characterized by very high stability and correctness. The intra-laboratory quality control system using reference strains is a useful tool for monitoring and supervising the method and laboratory personnel competency performing identification tests during routine microbiological work.

scholarly journals Detection of Structural and Conformational Changes in ALS-Causing Mutant Profilin1 With Hydrogen/Deuterium Exchange Mass Spectrometry and Bioinformatics Techniques

2021 ◽  
Author(s):  
Ahmad Shahir Sadr ◽  
zahra abdollahpour ◽  
Atousa Aliahmadi ◽  
Changiz Eslahchi ◽  
Mina Nekouei ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Amino Acid ◽  
Conformational Changes ◽  
Docking Simulation ◽  
Hydrogen Deuterium Exchange ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Hydrogen Deuterium ◽  
Tof Ms

Abstract The hydrogen/deuterium exchange (HDX) is a reliable method to survey the dynamic behavior of proteins and epitope mapping. Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS) is a quantifying tool to assay for HDX in the protein of interest. We combined HDX-MALDI-TOF MS and molecular docking/MD simulation to identify accessible amino acids and analyze their contribution in the structural changes of profilin1 (PFN1). The molecular docking/MD simulations are computational tools for enabling the analysis of the type of amino acids that may be involved via HDX identified under the lowest binding energy condition. Glycine to Valine amino acid (G117V) substitution mutation is linked to amyotrophic lateral sclerosis (ALS). This mutation is found to be in the actin-binding site of PFN1 and prevents the dimerization/polymerization of actin and invokes a pathologic toxicity that leads to ALS. In this study, we sought to understand the PFN1 protein dynamic behavior using purified wild type and mutant PFN1 proteins. The data obtained from HDX-MALDI-TOF MS for PFN1WT and PFN1G117V at various time intervals, from seconds to hours, revealed multiple peaks corresponding to molecular weights from monomers to multimers. PFN1/Benzaldehyde complexes identified 20 accessible amino acids to HDX that participate in the docking simulation in the surface of WT and mutant PFN1. Consistent results from HDX-MALDI-TOF MS and docking simulation predict candidate amino acid(s) involved in the dimerization/polymerization of PFNG117V. This information may shed critical light on the structural and conformational changes with details of amino acid epitopes for mutant PFN1s’ dimerization, oligomerization, and aggregation.

scholarly journals Outbreak of botulism type A in dairy cows detected by MALDI-TOF mass spectrometry

2020 ◽  
Vol 32 (5) ◽  
pp. 722-726
Author(s):  
Elisha A. Frye ◽  
Christina Egan ◽  
Michael J. Perry ◽  
Esther E. Crouch ◽  
Kyle E. Burbank ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
New York ◽  
New York State ◽  
Clinical Signs ◽  
Type A ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Botulinum Type ◽  
Type C ◽  
Tof Ms

Twenty-eight lactating dairy cattle in New York State were exposed to botulism toxin; 12 died and 16 recovered but never returned to full productivity. Pieces of a raccoon carcass were found in the total mixed ration on the first day of the outbreak. Clinical signs included anorexia, decreased milk production, decreased tongue tone, profound weakness, and recumbency. Clostridium botulinum type A (BoNT/A) was detected in rumen contents from 2 deceased cows via matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). In addition, C. botulinum type C was cultured from the liver of a third cow, and C. botulinum neurotoxin-producing type C gene ( bont/C) was detected via real-time PCR. On postmortem examination, 4 cows had findings suggestive of toxic myopathy, but the cause and significance of these lesions is unknown given that botulism is typically not associated with gross or histologic lesions. This outbreak of BoNT/A in cattle in North America was diagnosed via MALDI-TOF MS, a rapid and sensitive modality for detection of botulinum preformed neurotoxin.

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