PXD016511

PXD016511 is an original dataset announced via ProteomeXchange.

Title	Proteomic adaptation of Streptococcus pneumoniae to the human antimicrobial peptide LL-37
Description	Secreted antimicrobial peptides (AMPs) are an important part of the human innate immune system and prevent local and systemic infections by inhibiting bacterial growth in a concentration dependent manner. In the respiratory tract, the cationic peptide LL-37 is one of the most abundant AMPs and capable of building pore complexes in usually negatively charged bacterial membranes, leading to destruction of bacteria. However, adaptation mechanisms of several pathogens to LL-37 are already described and are known to weaken the antimicrobial effect of the AMP, for instance, by repulsion, export or degradation of the peptide. This study examines proteome wide changes in Streptococcus pneumoniae D39, the leading cause of bacterial pneumonia, in response to physiological concentrations of LL-37 by high resolution mass spectrometry. Our data indicate that pneumococci may use some of the known adaptation mechanisms to reduce the effect of LL-37 on their physiology, too. Additionally, several proteins seem to be involved in resistance to AMPs which have not been related to this process before, such as the teichoic acid flippase TacF (SPD_1128). Understanding colonization and infection relevant adaptations of the pneumococcus to AMPs, especially LL-37, could finally uncover new drug targets to weaken the burden of this widespread pathogen.
HostingRepository	PRIDE
AnnounceDate	2020-11-05
AnnouncementXML	Submission_2020-11-05_02:15:39.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Pierre-Alexander Mücke
SpeciesList	scientific name: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466); NCBI TaxID: 373153;
ModificationList	iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2019-11-28 08:04:10	ID requested
1	2020-03-19 16:46:42	announced
2	2020-03-24 05:25:33	announced	2020-03-24: Updated publication reference for PubMed record(s): 32183275.
⏵ 3	2020-11-05 02:15:40	announced	2020-11-05: Updated project metadata.

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]

curator keyword: Biomedical

submitter keyword: Streptococcus pneumoniae, antimicrobial peptide, LL-37, adaptation, LC-MSMS

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

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/2020/03/PXD016511

PRIDE project URI

• PRIDE
  1. PXD016511
     1. Label: PRIDE project
     2. Name: Proteomic adaptation of Streptococcus pneumoniae to the human antimicrobial peptide LL-37