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. 2023 Aug 3;18(8):e0289308.
doi: 10.1371/journal.pone.0289308. eCollection 2023.

Peptide barcode of multidrug-resistant strains of Neisseria gonorrhoeae isolated from patients in Thailand

Sittiruk Roytrakul  1 , Pongsathorn Sangprasert  2 , Janthima Jaresitthikunchai  1 , Narumon Phaonakrop  1 , Teerakul Arpornsuwan  3
Affiliations

Peptide barcode of multidrug-resistant strains of Neisseria gonorrhoeae isolated from patients in Thailand

Sittiruk Roytrakul et al. PLoS One. .

Abstract

The emergence of multidrug-resistant strains of Neisseria gonorrhoeae constitutes a serious threat to public health. The present study aimed to investigate peptidome-based biomarkers of multidrug-resistant N. gonorrhoeae, using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and liquid chromatography tandem mass spectrometry (LC-MS). The peptide barcode database of multidrug resistant N. gonorrhoeae was generated from the whole-cell peptides of 93 N. gonorrhoeae isolated from patients in Thailand. The dendrogram of 93 independent isolates of antibiotic-resistant N. gonorrhoeae revealed five distinct clusters including azithromycin resistance group (AZ), ciprofloxacin resistance group (C), ciprofloxacin and penicillin resistance group (CP), ciprofloxacin and tetracycline resistance group (CT), ciprofloxacin, penicillin and tetracycline resistance group (CPT). The peptidomes of all clusters were comparatively analyzed using a high-performance liquid chromatography-mass spectrometry method (LC-MS). Nine peptides derived from 9 proteins were highly expressed in AZ (p value < 0.05). These peptides also played a crucial role in numerous pathways and showed a strong relationship with the antibiotic resistances. In conclusion, this study showed a rapid screening of antibiotic-resistant N. gonorrhoeae using MALDI-TOF MS. Additionally, potential specific peptidome-based biomarker candidates for AZ, C, CP, CT and CPT-resistant N. gonorrhoeae were identified.

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1. Dendrogram and MALDI-TOF peptide barcodes of 93 multidrug resistant N. gonorrhoeae clinical isolates.
(A) Dendrogram of Hierarchical Cluster Analysis based on the peptide barcodes. (B) Average MALDI-TOF peptide barcodes of azithromycin resistance (AZ), ciprofloxacin resistance (C), ciprofloxacin and penicillin resistance (CP), ciprofloxacin and tetracycline resistance (CT), ciprofloxacin, penicillin and tetracycline resistance (CPT). The X-axis represents the mass to charge ratio (m/z) and the Y-axis represents the intensity of the spectra.
Fig 2
Fig 2. A heatmap of differentially expressed peptides in multidrug resistant N. gonorrhoeae.
Peptides expressed differentially in azithromycin resistance (AZ), ciprofloxacin resistance (C), ciprofloxacin and penicillin resistance (CP), ciprofloxacin and tetracycline resistance (CT), ciprofloxacin, penicillin and tetracycline resistance (CPT). The peptidome analysis was done in triplicate.
Fig 3
Fig 3. A principal component analysis (PCA) of multidrug resistant N. gonorrhoeae peptidome.
Separation of peptide profiles of azithromycin resistance (AZ), ciprofloxacin resistance (C), ciprofloxacin and penicillin resistance (CP), ciprofloxacin and tetracycline resistance (CT), ciprofloxacin, penicillin and tetracycline resistance (CPT). The peptidome analysis was done in triplicate.
Fig 4
Fig 4. Distribution of peptides identified in multidrug resistant N. gonorrhoeae.
A Venn diagram of 9 peptides significantly expressed in azithromycin resistance (AZ), ciprofloxacin resistance (C), ciprofloxacin and penicillin resistance (CP), ciprofloxacin and tetracycline resistance (CT), ciprofloxacin, penicillin and tetracycline resistance (CPT).
Fig 5
Fig 5. Association of peptides identified in multidrug resistant N. gonorrhoeae.
Involvements of amino acid permease ATP-binding protein (NLA_15390), carbamoyl-phosphate synthase large chain (carB), phosphoglycerate kinase (pgk), PilC protein (PilC), polyphosphate kinase (ppk), pyrroline-5-carboxylate reductase (proC), transferrin-binding protein B (tbpB), and transketolase (tkt) in networks of protein–antibiotic agent interactions: azithromycin, ciprofloxacin, penicillin and tetracycline.
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