ArticleJournal of molecular evolution2015
Adaptive evolution of formyl peptide receptors in mammals.
Article in Journal of molecular evolution, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- Involvement of formyl peptide receptor 2 in canine coronavirus infection: in vitro and in Silico approaches.Virology journal · 2025Article
- Chemosensory Receptors in Vertebrates: Structure and Computational Modeling Insights.International journal of molecular sciences · 2025Review
- Formyl peptide receptor 2: a potential therapeutic target for inflammation-related diseases.Pharmacological reports : PR · 2025Review
- TheFrontiers in immunology · 2025Review
- Dynamic Evolution of Bacterial Ligand Recognition by Formyl Peptide Receptors.Genome biology and evolution · 2023Article
- Caulerpin MitigatesInternational journal of molecular sciences · 2021Article
- Formyl peptide receptor 2, as an important target for ligands triggering the inflammatory response regulation: a link to brain pathology.Pharmacological reports : PR · 2021Review
- From immune to olfactory expression: neofunctionalization of formyl peptide receptors.Cell and tissue research · 2021Article
- Comparative genomic analyses illuminate the distinct evolution of megabats within Chiroptera.DNA research : an international journal for rapid publication of reports on genes and genomes · 2020Article
- TheNeural regeneration research · 2020Review
- Article
- Unusual sequence characteristics of human chromosome 19 are conserved across 11 nonhuman primates.BMC evolutionary biology · 2020Article
- The Contribution of Formyl Peptide Receptor Dysfunction to the Course of Neuroinflammation: A Potential Role in the Brain Pathology.Current neuropharmacology · 2020Review
- Formyl peptide receptor 2 regulates monocyte recruitment to promote intestinal mucosal wound repair.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- FPR1 is the plague receptor on host immune cells.Nature · 2019Article
- Large Scale Analyses and Visualization of Adaptive Amino Acid Changes Projects.Interdisciplinary sciences, computational life sciences · 2018Article
- Formyl-peptide receptor 2 governs leukocyte influx in localFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Mechanistic insights into molecular evolution of species-specific differential glycosaminoglycan binding surfaces in growth-related oncogene chemokines.Royal Society open science · 2017Article
- The Formyl Peptide Receptors: Diversity of Ligands and Mechanism for Recognition.Molecules (Basel, Switzerland) · 2017Review
- Molecular Evolution of the TET Gene Family in Mammals.International journal of molecular sciences · 2015Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formyl peptide receptors (FPRs) are a family of chemoattractant receptors with important roles in host defense and the regulation of inflammatory reactions. In humans, three FPR paralogs have been identified (FPR1, FPR2, and FPR3) and may have functionally diversified by gene duplication and adaptive evolution. However, the evolutionary mechanisms operating in the diversification of FPR family genes and the changes in selection pressures have not been characterized to date. Here, we have made a comprehensive evolutionary analysis of FPR genes from mammalian species. Phylogenetic analysis showed that an early duplication was responsible for FPR1 and FPR2/FPR3 splitting, and FPR3 originated from the latest duplication event near the origin of primates. Codon-based tests of positive selection reveal interesting patterns in FPR1 and FPR2 versus FPR3, with the first two genes showing clear evidence of positive selection at some sites while the majority of them evolve under strong negative selection. In contrast, our results suggest that the selective pressure may be relaxed in the FPR3 lineage. Of the six amino acid sites inferred to evolve under positive selection in FPR1 and FPR2, four sites were located in extracellular loops of the protein. The electrostatic potential of the extracellular surface of FPR might be affected more frequently with amino acid substitutions in positively selected sites. Thus, positive selection of FPRs among mammals may reflect a link between changes in the sequence and surface structure of the proteins and is likely to be important in the host's defense against invading pathogens.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.