ArticleProceedings of the National Academy of Sciences of the United States of America2014
Methylated glycans as conserved targets of animal and fungal innate defense.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 87 citations in OpenAlex.
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- Golgi-localized putative S-adenosyl methionine transporters required for plant cell wall polysaccharide methylation.Nature plants · 2022Article
- Expanding the Biological Role of Lipo-Chitooligosaccharides and Chitooligosaccharides inFrontiers in fungal biology · 2022Article
- A Comprehensive Phylogenetic and Bioinformatics Survey of Lectins in the Fungal Kingdom.Journal of fungi (Basel, Switzerland) · 2021Article
- The Role of Fucose-Containing Glycan Motifs Across Taxonomic Kingdoms.Frontiers in molecular biosciences · 2021Article
- Review
- Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family.Molecules (Basel, Switzerland) · 2019Article
- Comparisons of N-glycans across invertebrate phyla.Parasitology · 2019Review
- Bis-naphthopyrone pigments protect filamentous ascomycetes from a wide range of predators.Nature communications · 2019Article
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14 authors at 4 institutions in 3 countries.
Funding
Abstract
Effector proteins of innate immune systems recognize specific non-self epitopes. Tectonins are a family of β-propeller lectins conserved from bacteria to mammals that have been shown to bind bacterial lipopolysaccharide (LPS). We present experimental evidence that two Tectonins of fungal and animal origin have a specificity for O-methylated glycans. We show that Tectonin 2 of the mushroom Laccaria bicolor (Lb-Tec2) agglutinates Gram-negative bacteria and exerts toxicity toward the model nematode Caenorhabditis elegans, suggesting a role in fungal defense against bacteria and nematodes. Biochemical and genetic analysis of these interactions revealed that both bacterial agglutination and nematotoxicity of Lb-Tec2 depend on the recognition of methylated glycans, namely O-methylated mannose and fucose residues, as part of bacterial LPS and nematode cell-surface glycans. In addition, a C. elegans gene, termed samt-1, coding for a candidate membrane transport protein for the presumptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi was identified. Intriguingly, limulus lectin L6, a structurally related antibacterial protein of the Japanese horseshoe crab Tachypleus tridentatus, showed properties identical to the mushroom lectin. These results suggest that O-methylated glycans constitute a conserved target of the fungal and animal innate immune system. The broad phylogenetic distribution of O-methylated glycans increases the spectrum of potential antagonists recognized by Tectonins, rendering this conserved protein family a universal defense armor.
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