Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents

Staphylococcus aureus is a Gram-positive human pathogen that has developed resistance to all traditionally used antibiotics. Sortase A (SrtA) is a ‘house-keeping’ enzyme present in a number of Gram-positive organisms including S. aureus that is responsible for the covalent anchoring of proteins to t...

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Main Author: Tong, Carmen
Format: Thesis (University of Nottingham only)
Language:English
Published: 2018
Subjects:
Online Access:https://eprints.nottingham.ac.uk/53236/
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author Tong, Carmen
author_facet Tong, Carmen
author_sort Tong, Carmen
building Nottingham Research Data Repository
collection Online Access
description Staphylococcus aureus is a Gram-positive human pathogen that has developed resistance to all traditionally used antibiotics. Sortase A (SrtA) is a ‘house-keeping’ enzyme present in a number of Gram-positive organisms including S. aureus that is responsible for the covalent anchoring of proteins to the cell wall through the recognition of a highly conserved LPXTG motif. Many of the proteins it anchors are involved in virulence and immune evasion suggesting that it is an attractive target for potential anti-infective therapies. Moreover, as SrtA is not vital for bacterial growth or survival, inhibition may not select for the development of drug-resistance, unlike conventional antibiotics. This study evaluated different assays to assay SrtA activity and includes an in vitro Fluorescence Resonance Energy Transfer (FRET) assay using purified recombinant SrtA protein and an in vivo whole cell-based assay that measured SrtA-mediated anchoring of Gaussia luciferase (GLuc) in S. aureus. A further in vivo assay was evaluated, which measured SrtA activity using fluorescence as a reporter and analysis by flow cytometry and structured illumination microscopy. In this study three novel small molecules were identified as potential inhibitors of SrtA using in silico computational docking and SAR analysis; NCC-00014270, NCC-00076932 and NCC-00032784. These compounds were shown to inhibit SrtA in vitro in a dose-dependent manner with IC50s of 140 ± 24.6 µM, 172 ± 28.1 µM and 628 ± 122 µM respectively and were shown to act as competitive inhibitors of the SrtA. With the use of an in vivo reporter, it was shown that all three compounds negatively affected SrtA-mediated anchoring in S. aureus whole cells. Moreover, the cytotoxicity of these lead compounds against eukaryotic cells was assessed. Overall, these data suggest that two of the three lead compounds were potential ‘hit’ molecules for further structural modification for increased inhibitory activity against SrtA.
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spelling nottingham-532362025-02-28T14:12:11Z https://eprints.nottingham.ac.uk/53236/ Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents Tong, Carmen Staphylococcus aureus is a Gram-positive human pathogen that has developed resistance to all traditionally used antibiotics. Sortase A (SrtA) is a ‘house-keeping’ enzyme present in a number of Gram-positive organisms including S. aureus that is responsible for the covalent anchoring of proteins to the cell wall through the recognition of a highly conserved LPXTG motif. Many of the proteins it anchors are involved in virulence and immune evasion suggesting that it is an attractive target for potential anti-infective therapies. Moreover, as SrtA is not vital for bacterial growth or survival, inhibition may not select for the development of drug-resistance, unlike conventional antibiotics. This study evaluated different assays to assay SrtA activity and includes an in vitro Fluorescence Resonance Energy Transfer (FRET) assay using purified recombinant SrtA protein and an in vivo whole cell-based assay that measured SrtA-mediated anchoring of Gaussia luciferase (GLuc) in S. aureus. A further in vivo assay was evaluated, which measured SrtA activity using fluorescence as a reporter and analysis by flow cytometry and structured illumination microscopy. In this study three novel small molecules were identified as potential inhibitors of SrtA using in silico computational docking and SAR analysis; NCC-00014270, NCC-00076932 and NCC-00032784. These compounds were shown to inhibit SrtA in vitro in a dose-dependent manner with IC50s of 140 ± 24.6 µM, 172 ± 28.1 µM and 628 ± 122 µM respectively and were shown to act as competitive inhibitors of the SrtA. With the use of an in vivo reporter, it was shown that all three compounds negatively affected SrtA-mediated anchoring in S. aureus whole cells. Moreover, the cytotoxicity of these lead compounds against eukaryotic cells was assessed. Overall, these data suggest that two of the three lead compounds were potential ‘hit’ molecules for further structural modification for increased inhibitory activity against SrtA. 2018-12-13 Thesis (University of Nottingham only) NonPeerReviewed application/pdf en arr https://eprints.nottingham.ac.uk/53236/1/Carmen%20Tong%20PhD%20Thesis%202018.pdf Tong, Carmen (2018) Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents. PhD thesis, University of Nottingham. Sortase A Staphylococcus aureus Quorum sensing Anti-infective bioluminescence
spellingShingle Sortase A
Staphylococcus aureus
Quorum sensing
Anti-infective
bioluminescence
Tong, Carmen
Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents
title Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents
title_full Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents
title_fullStr Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents
title_full_unstemmed Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents
title_short Screening for inhibitors of Staphylococcal Sortase A as novel anti-infective agents
title_sort screening for inhibitors of staphylococcal sortase a as novel anti-infective agents
topic Sortase A
Staphylococcus aureus
Quorum sensing
Anti-infective
bioluminescence
url https://eprints.nottingham.ac.uk/53236/