title: Formylated MHC Class Ib Binding Peptides Activate Both Human and Mouse Neutrophils Primarily through Formyl Peptide Receptor 1.
abstract: Two different immune recognition systems have evolved in parallel to recognize peptides starting with an N-formylated methionine, and recognition similarities/differences between these two systems have been investigated. A number of peptides earlier characterized in relation to the H2-M3 complex that presents N-formylated peptides to cytotoxic T cells, have been characterized in relation to the formyl peptide receptors expressed by phagocytic neutrophils in both men (FPRs) and mice (Fprs). FPR1/Fpr1 was identified as the preferred receptor for all fMet-containing peptides examined, but there was no direct correlation between H2-M3 binding and the neutrophil activation potencies. Similarly, there was no direct correlation between the activities induced by the different peptides in human and mouse neutrophils, respectively. The formyl group was important in both H2-M3 binding and FPR activation, but FPR2 was the preferred receptor for the non-formylated peptide. The structural requirements differed between the H2-M3 and FPR/Fpr recognition systems and these data suggest that the two recognition systems have different evolutionary traits.
authors.affiliation: Department of Rheumatology and Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Malene
authors.initials: M
authors.lastname: Winther
authors.affiliation: Department of Rheumatology and Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
authors.forename: André
authors.initials: A
authors.lastname: Holdfeldt
authors.affiliation: Department of Rheumatology and Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Michael
authors.initials: M
authors.lastname: Gabl
authors.affiliation: Center for Cancer Research, Frederick National Laboratory for Cancer Research, Frederick, Maryland, United States of America.
authors.forename: Ji Ming
authors.initials: JM
authors.lastname: Wang
authors.affiliation: Department of Rheumatology and Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Huamei
authors.initials: H
authors.lastname: Forsman
authors.affiliation: Department of Rheumatology and Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Claes
authors.initials: C
authors.lastname: Dahlgren
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015870:Gene Expression; D006801:Humans; D051379:Mice; D008810:Mice, Inbred C57BL; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000138:chemical synthesis / Q000494:pharmacology*; D019255:NADPH Oxidases / Q000235:genetics / Q000276:immunology; D018375:Neutrophil Activation / Q000187:drug effects; D009504:Neutrophils / Q000166:cytology / Q000187:drug effects* / Q000276:immunology; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology*; D061251:Primary Cell Culture; D044042:Receptors, Formyl Peptide / Q000819:agonists / Q000235:genetics / Q000276:immunology*; D013481:Superoxides / Q000819:agonists / Q000276:immunology
chemical_list: C469986:FPR1 protein, human; C469988:Fpr1 protein, mouse; C408902:MHC binding peptide; D009842:Oligopeptides; D044042:Receptors, Formyl Peptide; D013481:Superoxides; D009240:N-Formylmethionine Leucyl-Phenylalanine; D019255:NADPH Oxidases