Formylated MHC Class Ib Binding Peptides Activate Both Human and Mouse Neutrophils Primarily through Formyl Peptide Receptor 1

• Published in: PloS one Vol. 11; no. 12; p. e0167529
• Main Authors: Winther, Malene, Holdfeldt, André, Gabl, Michael, Wang, Ji Ming, Forsman, Huamei, Dahlgren, Claes
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01.12.2016; Public Library of Science (PLoS)
• Subjects: Activation; Amino Acid Sequence; Amino acids; Animals; Binding; Biology and Life Sciences; Cell activation; Correlation; Cytotoxicity; Formyl peptide receptors; Formyl peptides; Gene Expression; Genetic aspects; Humans; Immune recognition; Immune system; Inflammation; Leukocytes (neutrophilic); Ligands; Listeria; Lymphocytes; Lymphocytes T; Major histocompatibility complex; Medical research; Medicine; Medicine and Health Sciences; Methionine; Mice; Mice, Inbred C57BL; Mycobacterium tuberculosis; N-Formylmethionine Leucyl-Phenylalanine - chemical synthesis; N-Formylmethionine Leucyl-Phenylalanine - pharmacology; NADPH Oxidases - genetics; NADPH Oxidases - immunology; Neutrophil Activation - drug effects; Neutrophils; Neutrophils - cytology; Neutrophils - drug effects; Neutrophils - immunology; Oligopeptides - chemical synthesis; Oligopeptides - pharmacology; Peptides; Phagocytes; Phenols; Physical Sciences; Physiological aspects; Primary Cell Culture; Receptors; Receptors, Formyl Peptide - agonists; Receptors, Formyl Peptide - genetics; Receptors, Formyl Peptide - immunology; Recognition; Research and Analysis Methods; Rheumatology; Superoxides - agonists; Superoxides - immunology; T cells; Tuberculosis; United States; Sweden
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0167529

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.