Exciting developments in the TGM story !
As well as our TGM1 CD44 co-receptor paper in PNAS last year (2023) we have two studies on TGM4 and TGM6 available on BioRχiv:
Singh, S.P., Smyth, D.J., Cunningham, K.T., Mukundan, A., Byeon, C.-H., Hinck, C.S., White, M.P.J., Ciancia, C., Wasowska, N., Sanders, A., Jin, R., Lilla, S., Zanivan, S., Schoenherr, C., Inman, G., van Dinther, M., ten Dijke, P., Hinck, A.P. and Maizels, R.M. (2024) The helminth TGF-β mimic, TGM-4, is a modular multivalent ligand that binds CD44, CD49d and TGFβ receptors to preferentially target myeloid cells. https://doi.org/10.1101/2023.11.13.566701
White, S.E, Schwartze, T.A., Mukundan, A., Schoenherr, C., Singh, S., van Dinther, M., Cunningham, K., White, M.P.J., Campion, T., Pritchard, J., Hinck, C.S., ten Dijke, P., Inman, G., Maizels, R.M. and Hinck, A.P. (2024) TGM6, a secretory product of the helminth H. polygyrus, mimics TGF-β binding to TβRII to block signaling in fibroblasts. https://doi.org/10.1101/2023.12.22.573140
We also published last year an analysis of the evolution of the TGM protein family
Maizels, R.M. and Newfeld, S. (2023) Convergent evolution in a murine intestinal parasite rapidly created the TGM family of molecular mimics to suppress the host immune response. Genome Biology and Evolution 15:evad158. doi: 10.1093/gbe/evad158. PDF