Journal: Genome Biology and Evolution

Article Title: Dynamic Evolution of Bacterial Ligand Recognition by Formyl Peptide Receptors

doi: 10.1093/gbe/evad175

Figure Lengend Snippet: Loss of FPR1 in New World primates. ( A ) Evidence for inactivating mutations in FPR1 within the New World monkey lineage. Saimiri boliviensis displayed the most significant degeneration in this region, encoding only a short 271 nucleotide sequence with significant FPR1 similarity and no apparent start or stop codons. ( B ) Conserved synteny of the FPR gene cluster across New World monkeys.

Article Snippet: Surface expression was verified for FPR1 using Thermo Fisher FPR1 polyclonal antibody (PA5-33534), and cell lines with comparable cell surface expression were used for binding experiments.

Techniques: Sequencing

Journal: Genome Biology and Evolution

Article Title: Dynamic Evolution of Bacterial Ligand Recognition by Formyl Peptide Receptors

doi: 10.1093/gbe/evad175

Figure Lengend Snippet: Evidence of repeated positive selection acting on extracellular domains of primate and carnivore FPRs. Sites in ( A ) primate FPR1, ( B ) primate FPR2, and ( C ) carnivore FPR2 with elevated dN/dS as determined by PAML and HyPhy. Residues of the transmembrane domain are denoted in yellow on the protein diagram, with the majority of high dN/dS sites (teal) located in the extracellular (top) ligand-binding loops. Species used for phylogenetic analyses and are indicated in the phylogenies for each gene. Sites in with elevated dN/dS as determined by PAML and HyPhy are denoted with black arrows in the amino acid alignment.

Article Snippet: Surface expression was verified for FPR1 using Thermo Fisher FPR1 polyclonal antibody (PA5-33534), and cell lines with comparable cell surface expression were used for binding experiments.

Techniques: Selection, Ligand Binding Assay

Journal: Genome Biology and Evolution

Article Title: Dynamic Evolution of Bacterial Ligand Recognition by Formyl Peptide Receptors

doi: 10.1093/gbe/evad175

Figure Lengend Snippet: Rapidly evolving surfaces of FPRs contribute to predicted bacterial ligand binding. ( A ) i-TASSER predicted structures for human FPR1, bonobo FPR1, human FPR2, and cat FPR2. Sites exhibiting elevated dN/dS in the extracellular region are indicated in teal. Sites 170 and 190, which are polymorphic in human populations, are also indicated. ( B ) Multiple sequence alignment for sites under selection at FPR extracellular regions of interest. Divergent sites shown in purple highlight differences between human and bonobo FPR1. Sites under selection are indicated by teal (FPR1) and gray (FPR2) arrows. ( C ) Predicted structures of FPR1 reveal an occluding structure that may affect binding of FLIPR-like. Site 170, which is variable between humans and bonobos, is highlighted in teal.

Article Snippet: Surface expression was verified for FPR1 using Thermo Fisher FPR1 polyclonal antibody (PA5-33534), and cell lines with comparable cell surface expression were used for binding experiments.

Techniques: Ligand Binding Assay, Sequencing, Selection, Binding Assay