PXD020968-1

PXD020968 is an original dataset announced via ProteomeXchange.

Title	Proteomic adaptation of Streptococcus pneumoniae to the antimicrobial peptide human Beta Defensin 3 (hBD3) in comparison to other cell surface stresses
Description	The antimicrobial peptide human Beta Defensin 3 (hBD3) is an essential part of the innate immune system and involved in protection against respiratory pathogens by specifically permeabilizing bacterial membranes. The Gram-positive bacterium S. pneumoniae causes serious diseases including pneumonia, meningitis, and septicemia despite being frequently exposed to human defense molecules including hBD3 during colonization and infection. Thus, the question arises how pneumococci adapt to stress caused by antimicrobial peptides. We addressed this subject by analyzing the proteome of S. pneumoniae after treatment with hBD3 and compared our data with the proteomic changes induced by LL-37, another crucial antimicrobial peptide present in the human respiratory tract. As antimicrobial peptides usually cause membrane perturbations, the response to the membrane active cationic detergent cetyl trimethyl ammonium bromide (CTAB) was examined to assess the specificity of the pneumococcal response to antimicrobial peptides. In brief, hBD3 and LL-37 induce a similar response in pneumococci especially in changes of proteins with annotated transporter and virulence function. However, LL-37 causes changes in abundance of cell surface modification proteins that cannot be observed after treatment with hBD3. Interestingly, CTAB induces unique proteomic changes in S. pneumoniae. Though, the detergent seems to activate a two-component system that is also activated in response to antimicrobial peptide stress (TCS 05). Overall, our publicly available data represent a novel resource on pneumococcal adaptation to specific cell surface stresses on a functional level. This knowledge can potentially be used to develop strategies to circumvent pneumococcal resistance to antimicrobial peptides.
HostingRepository	PRIDE
AnnounceDate	2020-11-02
AnnouncementXML	Submission_2020-11-01_22:44:32.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Pierre-Alexander Mücke
SpeciesList	scientific name: Streptococcus pneumoniae D39; NCBI TaxID: 373153;
ModificationList	iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2020-08-18 04:01:52	ID requested
⏵ 1	2020-11-01 22:44:33	announced
2	2020-11-02 00:01:18	announced	2020-11-02: Updated project metadata.
3	2020-11-04 23:17:18	announced	2020-11-02: Updated project metadata. 2020-11-05: Updated publication reference for PubMed record(s): 33143252.

M, ü, cke PA, Maa, ß S, Kohler TP, Hammerschmidt S, Becher D, to the Human Antimicrobial Peptide LL-37. Microorganisms, 8(3):(2020) [pubmed]

submitter keyword: Streptococcus pneumoniae, antimicrobial peptides, hBD3, LL-37, adaptation, proteomics

Dörte Becher
contact affiliation	Department of Microbial Proteomics, Institute of Microbiology, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Straße 8, 17489 Greifswald, Germany
contact email	dbecher@uni-greifswald.de
lab head
Pierre-Alexander Mücke
contact affiliation	Department of Microbial Proteomics, Institute of Microbiology, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Straße 8, 17489 Greifswald, Germany
contact email	pierre.muecke@uni-greifswald.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD020968
     1. Label: PRIDE project
     2. Name: Proteomic adaptation of Streptococcus pneumoniae to the antimicrobial peptide human Beta Defensin 3 (hBD3) in comparison to other cell surface stresses