AmiA and AliA peptide ligands are secreted by Klebsiella pneumoniae and inhibit growth of Streptococcus pneumoniae

Lux, Janine; Holivololona, Lalaina; San Millan Gutierrez, Raquel; Hilty, Markus; Ramette, Alban; Heller, Manfred; Hathaway, Lucy J (2022). AmiA and AliA peptide ligands are secreted by Klebsiella pneumoniae and inhibit growth of Streptococcus pneumoniae. Scientific reports, 12(1), p. 22268. Springer Nature 10.1038/s41598-022-26838-z

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Streptococcus pneumoniae colonizes the human nasopharynx, a multi-species microbial niche. Pneumococcal Ami-AliA/AliB oligopeptide permease is an ABC transporter involved in environmental sensing with peptides AKTIKITQTR, FNEMQPIVDRQ, and AIQSEKARKHN identified as ligands of its substrate binding proteins AmiA, AliA, and AliB, respectively. These sequences match ribosomal proteins of multiple bacterial species, including Klebsiella pneumoniae. By mass spectrometry, we identified such peptides in the Klebsiella pneumoniae secretome. AmiA and AliA peptide ligands suppressed pneumococcal growth, but the effect was dependent on peptide length. Growth was suppressed for diverse pneumococci, including antibiotic-resistant strains, but not other bacterial species tested, with the exception of Streptococcus pseudopneumoniae, whose growth was suppressed by the AmiA peptide ligand. By multiple sequence alignments and protein and peptide binding site predictions, for AmiA we have identified the location of an amino acid in the putative binding site whose mutation appears to result in loss of response to the peptide. Our results indicate that pneumococci sense the presence of Klebsiella pneumoniae peptides in the environment.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DCR Services > Core Facility Massenspektrometrie- und Proteomics-Labor
04 Faculty of Medicine > Service Sector > Institute for Infectious Diseases
04 Faculty of Medicine > Service Sector > Institute for Infectious Diseases > Research

Graduate School:

Graduate School for Cellular and Biomedical Sciences (GCB)

UniBE Contributor:

Lux, Janine, Holivololona, Lalaina, San Millan Gutierrez, Raquel, Hilty, Markus, Ramette, Alban Nicolas, Heller, Manfred, Hathaway, Lucy Jane

Subjects:

600 Technology > 610 Medicine & health
500 Science > 570 Life sciences; biology

ISSN:

2045-2322

Publisher:

Springer Nature

Funders:

[4] Swiss National Science Foundation

Language:

English

Submitter:

Lucy Jane Hathaway

Date Deposited:

05 Jan 2023 14:39

Last Modified:

08 Jan 2023 02:11

Publisher DOI:

10.1038/s41598-022-26838-z

PubMed ID:

36564446

BORIS DOI:

10.48350/176683

URI:

https://boris.unibe.ch/id/eprint/176683

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