Abstract
Cross-kingdom mimicry of the receptor signaling and leukocyte recruitment activity of a human cytokine by its plant orthologs
Highlights
The nucleotide and amino acid sequences of AtMDL1, AtMDL2, and AtMDL3 were retrieved from UniProt and the European Nucleotide Archive (ENA) database
The A. thaliana MIF/D-DT–like (MDL) proteins (AtMDLs) share a sequence identity of 28 –33% with HsMIF; this value is similar to the homology between human migration-inhibitory factor (MIF) and its paralog D-DT/MIF-2
As the yeast CXCR4-transformant experiments implied a role in the activation of signal transduction, we focused on CXCR4 for subsequent functional studies and asked whether AtMDLs would trigger MIF-like CXCR4-facilitated signaling responses in mammalian cells
Summary
Cross-kingdom mimicry of the receptor signaling and leukocyte recruitment activity of a human cytokine by its plant orthologs. Human macrophage migration-inhibitory factor (MIF) is an evolutionarily-conserved protein that has both extracellular immune-modulating and intracellular cell-regulatory functions. MIF plays a role in various diseases, including inflammatory diseases, atherosclerosis, autoimmunity, and cancer It serves as an inflammatory cytokine and chemokine, and exhibits enzymatic activity. Plants possess MIF orthologs but lack the associated receptors, suggesting functional diversification across kingdoms. Recombinant Arabidopsis MDLs (AtMDLs) share similar secondary structure characteristics with human MIF, yet only have minimal residual tautomerase activity using either p-hydroxyphenylpyruvate or dopachrome methyl ester as substrate. AtMDLs bind to the human MIF receptors CD74 and CXCR4. The authors declare that they have no conflicts of interest with the contents of this article
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