Figure 1. RNH1 shares homology with multiple NLR proteins and is expressed in myeloid cells.

(A) Circular tree representing the domain conservation relationship of human RNH1. Protein sequence alignments were made using MAFFT. A maximum likelihood phylogenetic tree was generated using IQ-Tree with 1,000 bootstrap replicates. Internal tree scale is shown with circular grid. (B) Structural alignment of protein domains. The domain information of selected proteins taken from Uniprot and represented using Illustrator for Biological Sequences (IBS) tool. (C) Human healthy BM biopsies were stained with RNH1 antibody. Myeloid cells showing high RNH1 expression are indicated with arrows. Scale bar 100 μm. (D) BM biopsies from patients with confirmed inflammatory conditions were stained with RNH1 antibody. Myeloid cells with increased RNH1 expression are indicated with arrows. These patients were non–COVID-19 patients. Scale bar 100 μm. (E) THP1 cells were stimulated with TLR2 ligand Pam3CSK4 (1 μg/ml) for 24 h. Total protein lysates were isolated and analysed by Western blot with indicated antibodies. Blots are representative of two independent experiments. (F) Mouse primary BMDMs were stimulated with TLR4 ligand LPS (1 μg/ml) for 24 h. Total protein lysates were isolated and analysed by Western blot with indicated antibodies. Blots are representative of two independent experiments. NLRP (nucleotide-binding oligomerization domain, leucine-rich repeat and pyrin domain–containing protein), NACHT (nucleotide-binding oligomerization domain), LRR (leucine-rich repeat protein), CARD (caspase activation and recruitment domain), CARMIL1 (capping protein regulator and myosin 1 linker 1), PODN L1 (podocan like 1), LRRC31 (leucine-rich repeat containing 31), NOD1 (nucleotide-binding oligomerization domain containing 1), and FIIND (function to find domain).

Source data are available for this figure.