If it is methylated it must be Tectonic.

The molecular mechanisms by which organisms defend themselves against predators and the molecular weapons the predators use to attack their victims have coevolved over eons of time. Microbial pathogens share the common feature of being covered in a surface coat comprised of carbohydrates (glycans) linked to lipids and proteins or as free polysaccharides. In vertebrates, such defense mechanisms against microbes and parasites include anti-glycan antibodies (1–3), major histocompatibility complex MHCII (4), and MHCI-like molecules to glycolipids (5), as well as a vast army of innate immune receptors, including the pattern recognition receptors that include Toll-like receptors, NOD-like receptors, RIG-I-like receptors, AIM2-like receptors, DNA sensors, C-type lectin receptors, and galectins (6–12). Many of these receptor systems are required to eliminate infectious organisms, and they do so by either promoting their direct killing or through uptake and signaling to bring additional cell-mediated effector mechanisms to eliminate the threat. The search for additional mechanisms of anti-glycan responses has been heightened by new methods in glycosciences, whereby the glycans of both the hosts and their enemies are becoming defined, especially through the use of molecular genetics, MS, and NMR to identify the glycan-related genes and glycan structures they encode as secondary gene products. In PNAS, Wohlschlager et al. (13) present a very interesting and novel advance in this area through their discovery of the role of Tectonins in both fungi and animals in recognizing specific methylated glycans of both bacteria and nematodes (worms). Tectonins are ancient proteins originally discovered in the slime mold Physarum polycephalum and have been found to have homology to limulus lectins (Tachylectin-1) (14). Such proteins fall within the Tectonin domain-containing superfamily, which contains the 33–37 amino acid consensus Tectonin domain sequence that is predicted to form a fourto six-bladed β-propeller structure with each blade formed by a four-stranded antiparallel β-sheet (15). These proteins have been proposed to play key roles in innate immunity in invertebrates and a human Tectonin is proposed to also be important in innate immunity to pathogens (16). However, the exact specificity of Tectonins for glycan ligands has been unclear. Wohlschlager et al. find that Tectonin 2 from the ectomycorrhizal mushroom Laccaria bicolor (Lb-Tec2) agglutinated some Gramnegative bacteria and was cytotoxic for the free-living nematode Caenorhabditis elegans. Cytotoxity to C. elegans involved binding to intestinal cells in a similar fashion to other nematotoxic fungal lectins (17, 18). A variety of experimental approaches indicated that binding occurred to glycan receptors on the bacteria and nematode. The genome of L. bicolor contains several predicted Tectonin genes, but the authors focus on predicted proteins Tectonin 1 (LbTec1) and Tectonin 2 (LbTec2), both of which lack a signal sequence and are predicted cytoplasmic proteins and both of which contain six tandemly arranged Tectonin domains. The transcription of the gene encoding LbTec2