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

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 pr...

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Bibliographic Details
Published in:	Scientific reports Vol. 12; no. 1; p. 22268
Main Authors:	Lux, Janine, Holivololona, Lalaina, San Millan Gutierrez, Raquel, Hilty, Markus, Ramette, Alban, Heller, Manfred, Hathaway, Lucy J.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 23-12-2022 Nature Publishing Group Nature Portfolio
Subjects:	631/326 692/308 ABC transporter Amino acid sequence Amino acids Antibiotic resistance Bacterial Proteins - metabolism Binding sites Carrier Proteins - metabolism Humanities and Social Sciences Humans Klebsiella pneumoniae Klebsiella pneumoniae - metabolism Ligands Mass spectrometry Mass spectroscopy multidisciplinary Nasopharynx Oligopeptide permease Peptides Peptides - metabolism Peptides - pharmacology Permease Pneumococcal Infections Ribosomal proteins Science Science (multidisciplinary) Secretome Streptococcus infections Streptococcus pneumoniae Streptococcus pneumoniae - genetics
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2045-2322 2045-2322
DOI:	10.1038/s41598-022-26838-z