File Download
Links for fulltext
(May Require Subscription)
- Scopus: eid_2-s2.0-85088454570
- PMID: 32690818
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Characterisation of Staphylococcus aureus virulence factor EsxA and structure-based screening of EsxA inhibitors for combating methicillin-resistant S aureus: abridged secondary publication
Title | Characterisation of Staphylococcus aureus virulence factor EsxA and structure-based screening of EsxA inhibitors for combating methicillin-resistant S aureus: abridged secondary publication |
---|---|
Authors | |
Issue Date | 2020 |
Publisher | Hong Kong Academy of Medicine Press: Open Access Journals. The Journal's web site is located at http://www.hkmj.org/ |
Citation | Hong Kong Medical Journal, 2020, v. 26 n. 3, suppl. 4, p. 35-38 How to Cite? |
Abstract | 1. EsxB did not interact with EsxA by cell-free assays (ITC and NMR titration) and cell-based assays (coIP and pull-down). 2. Pull-down and NMR titration assays showed that EsxA was interacting with lipid mediators HOTrE and sphingosylphosphorylcholine, respectively. These results suggested that EsxA may function as a lipid mediator binding protein, and that EsxA is an immune evasion gene and provide important clue to delineate its mechanism of immune evasion. 3. A high performance platform was established for in silico structure-based screening against pathogen targets. The EsxA X-ray structure was subjected to structure-based screening with a ligand library containing 6.8 million lead-like or active lead ligands. 4. Of the 100 highest-scoring compounds, five were validated by the secondary NMR titration screen. One hit compound (6058448) showed MIC at 25 μM level by broth microdilution test, and another hit compound (5674203) also showed antivirulence effects by inhibiting the expression of both protein A and alpha-toxin of US300 strain. |
Persistent Identifier | http://hdl.handle.net/10722/300256 |
ISSN | 2023 Impact Factor: 3.1 2023 SCImago Journal Rankings: 0.261 |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sze, KH | - |
dc.contributor.author | Kao, RYT | - |
dc.date.accessioned | 2021-06-04T08:40:22Z | - |
dc.date.available | 2021-06-04T08:40:22Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Hong Kong Medical Journal, 2020, v. 26 n. 3, suppl. 4, p. 35-38 | - |
dc.identifier.issn | 1024-2708 | - |
dc.identifier.uri | http://hdl.handle.net/10722/300256 | - |
dc.description.abstract | 1. EsxB did not interact with EsxA by cell-free assays (ITC and NMR titration) and cell-based assays (coIP and pull-down). 2. Pull-down and NMR titration assays showed that EsxA was interacting with lipid mediators HOTrE and sphingosylphosphorylcholine, respectively. These results suggested that EsxA may function as a lipid mediator binding protein, and that EsxA is an immune evasion gene and provide important clue to delineate its mechanism of immune evasion. 3. A high performance platform was established for in silico structure-based screening against pathogen targets. The EsxA X-ray structure was subjected to structure-based screening with a ligand library containing 6.8 million lead-like or active lead ligands. 4. Of the 100 highest-scoring compounds, five were validated by the secondary NMR titration screen. One hit compound (6058448) showed MIC at 25 μM level by broth microdilution test, and another hit compound (5674203) also showed antivirulence effects by inhibiting the expression of both protein A and alpha-toxin of US300 strain. | - |
dc.language | eng | - |
dc.publisher | Hong Kong Academy of Medicine Press: Open Access Journals. The Journal's web site is located at http://www.hkmj.org/ | - |
dc.relation.ispartof | Hong Kong Medical Journal | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Characterisation of Staphylococcus aureus virulence factor EsxA and structure-based screening of EsxA inhibitors for combating methicillin-resistant S aureus: abridged secondary publication | - |
dc.type | Article | - |
dc.identifier.email | Sze, KH: khsze@HKUCC-COM.hku.hk | - |
dc.identifier.email | Kao, RYT: rytkao@hkucc.hku.hk | - |
dc.identifier.authority | Sze, KH=rp00785 | - |
dc.identifier.authority | Kao, RYT=rp00481 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.pmid | 32690818 | - |
dc.identifier.scopus | eid_2-s2.0-85088454570 | - |
dc.identifier.hkuros | 322723 | - |
dc.identifier.volume | 26 | - |
dc.identifier.issue | 3, suppl. 4 | - |
dc.identifier.spage | 35 | - |
dc.identifier.epage | 38 | - |
dc.publisher.place | Hong Kong | - |