Rapid diagnosis of periodontitis, a feasibility study using MALDI-TOF mass spectrometry

Abstract

The aim of the present study was to assess the feasibility and diagnostic contribution of protein profiling using MALDI-TOF mass spectrometry applied to saliva, gingival crevicular fluid (GCF) and dental plaque from periodontitis and healthy subjects. We hypothesized that rapid routine and blinded MALDI-TOF analysis could accurately classify these three types of samples according to periodontal state. Materials and methods Unstimulated saliva, GCF and dental plaque, collected from periodontitis subjects and healthy controls, were analyzed by MALDI-TOF MS. Based on the differentially expressed peaks between the two groups, diagnostic decision trees were built for each sample. Results Among 141 patients (67 periodontitis and 74 healthy controls), the decision trees diagnosed periodontitis with a sensitivity = 70.3% (± 0.211) and a specificity = 77.8% (± 0.165) for saliva, a sensitivity = 79.6% (± 0.188) and a specificity = 75.7% (± 0.195) for GCF, and a sensitivity = 72.1% (± 0.202) and a specificity = 72.2% (± 0.195) for dental plaque. The sensitivity and specificity of the tests were improved to 100% (CI 95% = [0.91;1]) and 100% (CI 95% = [0.92;1]), respectively, when two samples were tested. Conclusion We developed, for the first time, diagnostic tests based on protein profiles of saliva, GCF and dental plaque between periodontitis patients and healthy subjects. When at least 2 of these samples were tested, the best results were obtained.

A Combined approach of MALDI-TOF Mass Spectrometry and multivariate analysis as a potential tool for the detection of SARS-CoV-2 virus in nasopharyngeal swabs

“…No reuse allowed without permission. assays need to be deployed now in an effort to accelerate our understanding of COVID-19 disease (Chin et al, 2020;Antezack et al, 2020).…”

Gingival Crevicular Fluid Peptidome Profiling in Healthy and in Periodontal Diseases

“…Generally, the peptide profiling investigations that we summarize in this review make use of surface enhanced laser desorption ionization (SELDI) [17,18] and matrix-assisted laser desorption ionization (MALDI)-MS [6,[19][20][21][22][23][24][25][26] approaches which result more suitable and easily applicable for the analysis of natural peptides of GCF (Table 1). However, few investigations based on electrospray ionization (ESI)-MS have also been carried out to explore peptidic components and small proteins found in GCF in a top-down fashion [27][28][29] (Table 1).…”

“…Peptidomics workflow, without a digestion step, allows to preserve the endogenous information of peptides from GCF, including post-translational modifications and proteolytic products. (21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35) and (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35), Fibrinopeptide B Generally, the peptide profiling investigations that we summarize in this review make use of surface enhanced laser desorption ionization (SELDI) [17,18] and matrix-assisted laser desorption ionization (MALDI)-MS [6,[19][20][21][22][23][24][25][26] approaches which result more suitable and easily applicable for the analysis of natural peptides of GCF (Table 1). However, few investigations based on electrospray ionization (ESI)-MS have also been carried out to explore peptidic components and small proteins found in GCF in a top-down fashion [27][28][29]…”

“…Some, but not many investigations based on MS have been performed to explore the GCF peptidome both under physiological [20,22,23,27,28] and pathological conditions [6,[16][17][18][19]21,[24][25][26]29]. Targeted identifications of specific peptidic component in GCF have been reported by Lundy et al [16].…”

“…All these features make MALDI-TOF MS highly suitable for diagnostic purposes [59][60][61][62][63]. The versatility of the MALDI-TOF MS platform was exploited in different approaches to analyze GCF peptidome [6,[19][20][21][22][23][24][25][26].…”