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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| Published in: | Scientific reports Vol. 12; no. 1; p. 22268 |
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| Format: | Journal Article |
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| Abstract | 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. |
|---|---|
| AbstractList | 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. 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. Abstract 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. |
| ArticleNumber | 22268 |
| Author | Ramette, Alban Hilty, Markus Holivololona, Lalaina San Millan Gutierrez, Raquel Lux, Janine Hathaway, Lucy J. Heller, Manfred |
| Author_xml | – sequence: 1 givenname: Janine surname: Lux fullname: Lux, Janine organization: Institute for Infectious Diseases, Faculty of Medicine, University of Bern, Graduate School for Cellular and Biomedical Sciences, University of Bern – sequence: 2 givenname: Lalaina surname: Holivololona fullname: Holivololona, Lalaina organization: Institute for Infectious Diseases, Faculty of Medicine, University of Bern – sequence: 3 givenname: Raquel surname: San Millan Gutierrez fullname: San Millan Gutierrez, Raquel organization: Institute for Infectious Diseases, Faculty of Medicine, University of Bern – sequence: 4 givenname: Markus surname: Hilty fullname: Hilty, Markus organization: Institute for Infectious Diseases, Faculty of Medicine, University of Bern – sequence: 5 givenname: Alban surname: Ramette fullname: Ramette, Alban organization: Institute for Infectious Diseases, Faculty of Medicine, University of Bern – sequence: 6 givenname: Manfred surname: Heller fullname: Heller, Manfred organization: Proteomics and Mass Spectrometry Core Facility, Department for BioMedical Research (DBMR), University of Bern – sequence: 7 givenname: Lucy J. surname: Hathaway fullname: Hathaway, Lucy J. email: lucy.hathaway@unibe.ch organization: Institute for Infectious Diseases, Faculty of Medicine, University of Bern |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36564446$$D View this record in MEDLINE/PubMed |
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| Snippet | Streptococcus pneumoniae
colonizes the human nasopharynx, a multi-species microbial niche. Pneumococcal Ami-AliA/AliB oligopeptide permease is an ABC... Streptococcus pneumoniae colonizes the human nasopharynx, a multi-species microbial niche. Pneumococcal Ami-AliA/AliB oligopeptide permease is an ABC... Abstract Streptococcus pneumoniae colonizes the human nasopharynx, a multi-species microbial niche. Pneumococcal Ami-AliA/AliB oligopeptide permease is an ABC... |
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| SubjectTerms | 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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| Title | AmiA and AliA peptide ligands are secreted by Klebsiella pneumoniae and inhibit growth of Streptococcus pneumoniae |
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