Hence, the current knowledge on the functional role of methanoarchaea in the human intestine is mainly focused on bioenergetic aspects and Piperaquine tetraphosphate tetrahydrate syntrophic interactions with bacteria. However, few studies reported strong immunological properties of methanoarchaea after immunization of rabbits and mice. Thus, it is most likely that methanoarchaea are also capable to influence the community structure of the human gut microbiota through their interaction with blood immune cells or the mucosa itself. We report here on the inflammatory response of human moDCs to methanoarchaea and demonstrate that M. stadtmanae is capable to induce a markedly higher inflammatory cytokine response than M. smithii, and may represent a hitherto overlooked contributor to pathological conditions in the human intestine. Moreover, our data implicate the presence of a specific CGS-12066 maleate salt archaealassociated pattern recognition receptor in humans. Since members of the domain Archaea were not only found in the human intestine, but also in the oral cavity and in high abundance on human skin, archaeal strains may influence the overall human immune homeostasis to comparable extents as has been shown for bacteria. Consequently, there is an urgent need to include archaea in future studies regarding the role of the human microbiome. The structure consists of a short N-terminal intracellular region, a single N-terminal hydrophobic region that corresponds with the transmembrane domain, a highly conserved zinc-binding domain in exons 17 and 19, and a large extracellular C-terminal domain. The PHEX protein is predominantly expressed in cartilage, osteoblasts, and odontoblasts but not in the kidney. Although the exact mechanism of how PHEX mutations cause rickets/ osteomalacia remains unknown, some studies have shown that PHEX may inactivate bone mineralization inhibitors and that one of the extraosseous consequences of PHEX inactivation includes an increase in the level of FGF-23. In this study, we identified 10 different PHEX mutations in 16 patients from 9 unrelated families with XLH and reported the different clinical features observed in these Chinese patients. The nonsense mutations p.Trp660X in exon 20, p.Trp444X in exon 12, and p.Arg549X in exon 15 may result in the translation of truncated proteins that lack exons 20 to 22, exons 12 to 22, and exons 15 to 22, respectively. Four cysteine residues are located within this C-terminal region and are highly conserved in the PHEX protein.