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Structure of Mbp-Bte1 fusion proteinStructure of Mbp-Bte1 fusion protein
Structural highlights
FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Q5LDT7_BACFN Publication Abstract from PubMedAntagonistic interactions play a key role in determining microbial community dynamics. Here, we report that one of the most widespread contact-dependent effectors in human gut microbiomes, Bte1, directly targets the PpiD-YfgM periplasmic chaperone complex in related microbes. Structural, biochemical, and genetic characterization of this interaction reveals that Bte1 reverses the activity of the chaperone complex, promoting substrate aggregation and toxicity. Using Bacteroides, we show that Bte1 is active in the mammalian gut, conferring a fitness advantage to expressing strains. Recipient cells targeted by Bte1 exhibit sensitivity to membrane-compromising conditions, and human gut microbes can use this effector to exploit pathogen-induced inflammation in the gut. Further, Bte1 allelic variation in gut metagenomes provides evidence for an arms race between Bte1-encoding and immunity-encoding strains in humans. Together, these studies demonstrate that human gut microbes alter the protein-folding capacity of neighboring cells and suggest strategies for manipulating community dynamics. A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.,Lim B, Xu J, Wierzbicki IH, Gonzalez CG, Chen Z, Gonzalez DJ, Gao X, Goodman AL Cell Host Microbe. 2025 Jan 29:S1931-3128(25)00026-5. doi: , 10.1016/j.chom.2025.01.008. PMID:39909037[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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