biostudies-literatureMelicher FGrantová Agentura České RepublikyCALIPSOplusMinisterstvo Školství, Mládeže a Tělovýchovy1168-1190https://www.ebi.ac.uk/biostudies/studies/S-EPMC12914763biostudies-literatureUnknown293(4)Photorhabdus bacteria live in mutualistic relationships with Heterorhabditis nematodes, and together, they act as effective insect pathogens. These bacteria produce a diverse array of lectins, sugar-binding proteins that are believed to play crucial roles in the complex tripartite interaction among Photorhabdus, nematodes, and their insect hosts. One such lectin, Photorhabdus laumondii tumor necrosis factor (TNF)-like lectin (PLTL), identified in Photorhabdus laumondii subsp. laumondii TTO1, exhibits notable sequence similarity to the N-terminal domain of the BC2L-C lectin (BC2L-CN), a TNF-like lectin recognized for its specificity toward fucosylated glycans associated with human embryonic stem cells and certain cancers. Through glycan array analysis and surface plasmon resonance, we identThe FEBS journalStructural and functional characterization of the newly identified Photorhabdus laumondii tumor necrosis factor-like lectin.PMC1291476373087221‐29622SLM202304221-29622SMelicher FDobes PWimmerova MFaltinek LSykorova PKomarek JKorsak MHouser JfalseStructural and functional characterization of the newly identified Photorhabdus laumondii tumor necrosis factor-like lectin.Photorhabdus bacteria live in mutualistic relationships with Heterorhabditis nematodes, and together, they act as effective insect pathogens. These bacteria produce a diverse array of lectins, sugar-binding proteins that are believed to play crucial roles in the complex tripartite interaction among Photorhabdus, nematodes, and their insect hosts. One such lectin, Photorhabdus laumondii tumor necrosis factor (TNF)-like lectin (PLTL), identified in Photorhabdus laumondii subsp. laumondii TTO1, exhibits notable sequence similarity to the N-terminal domain of the BC2L-C lectin (BC2L-CN), a TNF-like lectin recognized for its specificity toward fucosylated glycans associated with human embryonic stem cells and certain cancers. Through glycan array analysis and surface plasmon resonance, we ident2026-01-01T00:00:00Z2026 Feb2026-07-16T06:51:21.961Z2026-07-09T10:41:12.762ZS-EPMC129147634110592210.1111/febs.70293