PXD035016-2

PXD035016 is an original dataset announced via ProteomeXchange.

Title	Biocontrol potentials and proteomic response of lipopeptide producing B. velezensis strains to Diaporthe spp.
Description	Lipopeptide biosurfactant producing Bacillus strains have many useful applications in biotechnology and agriculture, based on their emulsifying, surface activity and antimicrobial properties. In the current study, lipopeptide production kinetics, and biocontrol potentials of two new B. velezensis strains, ES1-02 and EFSO2-04 were analyzed and compared with those of commercial strains QST713 and FZB42. ES1-02 and EFSO2-04 showed higher specific growth rates than FZB42, but lower growth rates than QST713. All strains produced surfactin lipopetides, while fengycin production was not observed in ES1-02 and EFSO2-04. Production of fengycin A, B, X and Y were however confirmed in strains QST713 and FZB42. Significant differences were observed in the production of lipopeptides of the iturin family. While ES1-02 and EFSO2-04 produced bacillomycin L, QST713 produced iturin A, and FZB42 produced bacillomycin D. This was in line with the PCR analysis of corresponding genes encoding the identified lipopeptides. Highest surfactin titer of 97.4 mg/L was observed in ES1-02, while QST713 produced highest amount of iturin/bacillomycin (8.5 mg/L). Surfactin isoforms C12 to C17, and iturin/bacillomycin isoforms C11 to C17 were identified by mass spectrometry. ES1-02 and EFSO2-04 showed biocontrol potentials comparable with that of QST713 against Diaporthe spp., while FZB42 showed superior antifungal potentials. Up to 41%, 43%, 47 % and 68.9 % inhibition of D. caulivora were achieved by ES1-02, EFSO2-04, QST713 and FZB42 respectively. Upon exposure to B. velezensis strains, morphological changes to Diaporthe hyphae in form of swellings, distortion, and complete disruption occurred. Interaction of D. longicolla DPC_HOH20 with ES1-02 and EFSO2-04 induced 10-fold and 5-fold increase in surfactin synthesis, respectively. Antagonist interaction with D. longicolla induced significant changes in the proteome of ES1-02 including an increased abundance of several proteins associated with biosynthesis of antimicrobial compounds and fatty acids, while proteins associated with phosphate uptake were decreased in abundance.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:06:29.684.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jens Pfannstiel
SpeciesList	scientific name: Bacillus velezensis; NCBI TaxID: 492670; scientific name: Bacteria; NCBI TaxID: NCBITaxon:2;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2022-06-30 06:52:46	ID requested
1	2023-10-24 10:28:01	announced
⏵ 2	2023-11-14 09:06:30	announced	2023-11-14: Updated project metadata.
3	2024-10-22 06:07:56	announced	2024-10-22: Updated project metadata.

Akintayo SO, Hosseini B, Vahidinasab M, Messmer M, Pfannstiel J, Bertsche U, Hubel P, Henkel M, Hausmann R, Voegele RT, Lilge L, spp. Front Bioeng Biotechnol, 11():1228386(2023) [pubmed]

submitter keyword: Surfactin, Bacillus, Biocontrol, Lipopeptide, Antimicrobial, Fengycin,Agriculture, Proteomics, Bacillomycin, Iturin, LC-MS/MS

Dr. Lars Lilge
contact affiliation	Department of Bioprocess Engineering, Institute of Food Science and Biotechnology, University of Hohenheim, Fruwirthstr. 12, 70599 Stuttgart, Germany
contact email	lars.lilge@uni-hohenheim.de
lab head
Jens Pfannstiel
contact affiliation	University of Hohenheim
contact email	Jens.Pfannstiel@uni-hohenheim.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD035016
     1. Label: PRIDE project
     2. Name: Biocontrol potentials and proteomic response of lipopeptide producing B. velezensis strains to Diaporthe spp.