PXD050770 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Affinity-based protein profiling (AfBPP) using different Callyaerin probes in M. tuberculosis H37Rv |
Description | The natural cyclopeptide Callyaerin B (CalB) exhibits highly specific antitubercular activity. The aim of this project is to study the protein binding partner of this compound using either activity-based protein profiling (ABPP) (ACE_0721) or affinity-based protein profiling (AfBPP) (ACE_0682 & ACE_0721). To enable a two-step enrichment protocol, CalB probes modified with an alkyne group (CalB_C4Pra) and optionally additional photoleucine (CalB_R5phLeu) or 4-benzoyl-phenylalanine (CalB_R3Bpa) as photoactive groups were used. For this purpose, M. tuberculosis H37Rv cells were treated with the respective probe for three hours at 37 °C and then exposed to UV light (λ = 365 nM) for 20 minutes at room temperature. The cells were lysed, and biotin was attached to probe-labeled proteins using copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC). These proteins were subsequently enriched with an avidin-matrix, which was thoroughly washed with a 1% SDS solution. Furthermore, a competitive AfBPP approach was chosen, to distinguish specific protein labeling from background labeling (ACE_0721). For this, the cells were treated with excess of unmodified CalB for 30 minutes prior to the addition of the respective photoprobe. In addition, it has been shown, that the susceptibility of M. tuberculosis H37Rv to CalB is highly dependent on the expression of the putative membrane protein Rv2113. A gene deletion mutation of this protein (Δrv2113) was used to identify further unspecific labeling of the AfBPP approach (ACE_0740). |
HostingRepository | PRIDE |
AnnounceDate | 2024-07-25 |
AnnouncementXML | Submission_2024-07-25_10:27:55.077.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Farnusch Kaschani |
SpeciesList | scientific name: Mycobacterium tuberculosis H37Rv; NCBI TaxID: 83332; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-03-19 09:05:20 | ID requested | |
⏵ 1 | 2024-07-25 10:27:55 | announced | |
Publication List
10.1016/j.chembiol.2024.06.002; |
Podlesainski D, Adeniyi ET, Gr, ö, ner Y, Schulz F, Krisilia V, Rehberg N, Richter T, Sehr D, Xie H, Simons VE, Kiffe-Delf AL, Kaschani F, Ioerger TR, Kaiser M, Kalscheuer R, The anti-tubercular callyaerins target the Mycobacterium tuberculosis-specific non-essential membrane protein Rv2113. Cell Chem Biol, ():(2024) [pubmed] |
Keyword List
submitter keyword: Callyaerin |
Mycobacterium tuberculosis |
cyclopeptide |
natural product |
antibiotic action |
anti-TB drug development |
photoaffinity labelling |
Contact List
Farnusch Kaschani |
contact affiliation | Farnusch Kaschani, Analytics Core Facility Essen (ACE), Chemische Biologie, Universität Duisburg-Essen, ZMB, Germany |
contact email | farnusch.kaschani@uni-due.de |
lab head | |
Farnusch Kaschani |
contact affiliation | University Duisburg-Essen |
contact email | farnusch.kaschani@uni-due.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/07/PXD050770 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD050770
- Label: PRIDE project
- Name: Affinity-based protein profiling (AfBPP) using different Callyaerin probes in M. tuberculosis H37Rv