{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Coya JM"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["927017"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9493720"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["The exploration of therapies combining antimicrobial lung proteins and conventional antibiotics is important due to the growing problem of multidrug-resistant bacteria. The aim of this study was to investigate whether human SP-A and a recombinant trimeric fragment (rfhSP-A) have cooperative antimicrobial activity with antibiotics against pathogenic Gram-negative bacteria. We found that SP-A bound the cationic peptide polymyxin B (PMB) with an apparent dissociation constant (<i>K</i> <sub>D</sub>) of 0.32 ± 0.04 µM. SP-A showed synergistic microbicidal activity with polymyxin B and E, but not with other antibiotics, against three SP-A-resistant pathogenic bacteria: <i>Klebsiella pneumoniae</i>, non-typable <i>Haemophilus influenzae</i> (NTHi), and <i>Pseudomonas aeruginosa</i>. SP-A was not"],"journal":["Frontiers in immunology"],"pubmed_title":["Cooperative action of SP-A and its trimeric recombinant fragment with polymyxins against Gram-negative respiratory bacteria."],"pmcid":["PMC9493720"],"funding_grant_id":["BB/L007223/1","BB/T001976/1"],"pubmed_authors":["Garcia-Fojeda B","Casals C","Kronqvist N","Fraile-Agreda V","de Tapia L","Saenz A","Bengoechea JA","Coya JM","Johansson J"],"additional_accession":[]},"is_claimable":false,"name":"Cooperative action of SP-A and its trimeric recombinant fragment with polymyxins against Gram-negative respiratory bacteria.","description":"The exploration of therapies combining antimicrobial lung proteins and conventional antibiotics is important due to the growing problem of multidrug-resistant bacteria. The aim of this study was to investigate whether human SP-A and a recombinant trimeric fragment (rfhSP-A) have cooperative antimicrobial activity with antibiotics against pathogenic Gram-negative bacteria. We found that SP-A bound the cationic peptide polymyxin B (PMB) with an apparent dissociation constant (<i>K</i> <sub>D</sub>) of 0.32 ± 0.04 µM. SP-A showed synergistic microbicidal activity with polymyxin B and E, but not with other antibiotics, against three SP-A-resistant pathogenic bacteria: <i>Klebsiella pneumoniae</i>, non-typable <i>Haemophilus influenzae</i> (NTHi), and <i>Pseudomonas aeruginosa</i>. SP-A was not","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-04T21:34:58.266Z","creation":"2025-04-04T21:34:58.266Z"},"accession":"S-EPMC9493720","cross_references":{"pubmed":["36159837"],"doi":["10.3389/fimmu.2022.927017"]}}