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Five strains related to the genus Rodentibacter were isolated from five pet hamsters kept in Japan. Isolates were genotypically and phenotypically distinct from previously described species within the genus Rodentibacter (family Pasteurellaceae). The five strains were the most genetically similar to Rodentibacter haemolyticus 1625-19T, exhibiting a 16S rRNA gene sequence similarity of 96.5%, an average nucleotide identity value of 90.8% and a digital DNA–DNA hybridization value of 42.7%. Phenotypic characteristics further distinguish the isolated strains from other Rodentibacter species. Although they share β-haemolysis capacity with R. haemolyticus, the novel strains are differentiated by their positive reactions for α-glucosidase, l-arabinose and trehalose, as well as negative reactions for β-glucuronidase, mannose, inositol and glycerol. Genotypic and phenotypic differences between the novel strains and closely related known strains suggested that we have identified a new Rodentibacter species. We propose the name Rodentibacter abscessus sp. nov. The type strain is THUN1654T with a G+C DNA content of 40.6 mol%, and it is deposited in the DSMZ Germany (DSM 118002T), KCTC Korea (KCTC 8595T) and JCM Japan (JCM 37054T).

01 Mar 2025·Journal of Biological Chemistry

Txnip deficiency causes a susceptibility to acute cold stress with brown fat dysfunction in mice

Article

Author: Kagawa, Syota ; Masutani, Hiroshi ; Amo-Shiinoki, Kikuko ; Okuya, Shigeru ; Ikeda, Kenji ; Zou, Meng ; Ohta, Yasuharu ; Kohno, Daisuke ; Kitamura, Tadahiro ; Tanabe, Katsuya ; Shirasawa, Hideki ; Yamada, Tetsuya ; Tanizawa, Yukio ; Taguchi, Akihiko

Mammals adaptively regulate energy metabolism in response to environmental changes such as starvation and cold circumstances. Thioredoxin-interacting protein (Txnip), known as a redox regulator, serves as a nutrient sensor regulating energy homeostasis. Txnip is essential for mice to adapt to starvation, but its role in adapting to cold circumstances remains unclear. Here, we identified Txnip as a pivotal factor for maintaining nonshivering thermogenesis in mice. Txnip protein levels in brown adipose tissue (BAT) were upregulated by the acute cold exposure. Txnip-deficient (Txnip^-/-) mice acclimated to thermoneutrality (30 °C) exhibited significant BAT enlargement and triglyceride accumulation with downregulation of BAT signature and metabolic gene expression. Upon acute cold exposure (5 °C), Txnip^-/- mice showed a rapid decline in BAT surface temperatures with the failure of increasing metabolic respiration, developing lethal hypothermia. The BAT dysfunction and cold susceptibility in Txnip^-/- mice were corrected by acclimation to 16 °C, protecting the mice from life-threatening hypothermia. Transcriptomic and metabolomic analysis using dissected BAT revealed that despite preserving glycolysis, the BAT of Txnip^-/- mice failed to activate the catabolism of branched-chain amino acids and fatty acids in response to acute cold stress. These findings illustrate that Txnip is required for maintaining basal BAT function and ensuring cold-induced thermogenesis.

01 Mar 2025·Journal of Immunological Methods

Overcoming cross-reactivity of antibodies against human lactate dehydrogenase

Article

Author: Kondo, Akira ; Nakamura, Ayumu

Lactate dehydrogenase subunit A (LD-A) plays an important role in cancer regulation and therapy. We attempted to develop an enzyme-linked immune-solvent assay (ELISA) for LD-A in human serum. However, commercial antibodies against LD-A exhibited cross-reactivity with an unknown protein. The unknown protein was purified and characterized by protein sequencing and Western blotting. In addition, we attempted to prepare a specific antibody for the ELISA using partially synthesized peptides of LD-A as immunogens. The epitope position in LD-A was carefully selected based on bioinformatics analysis. Peptide sequencer elucidated a ten amino acid sequence of the purified protein at the N-terminal. A BLAST search revealed that this sequence perfectly matched that at the N-terminus of the IgG heavy chain (H-chain). Furthermore, we demonstrated that twelve commercially available antibodies targeting LD-A or LD-B (subunit B) primarily cross-reacted with IgG or its H-chain, with only one specific antibody for each subunit. As the specific antibody against LD-A is no longer commercially accessible, we successfully produced two kinds of specific antibodies using partially synthesized LD-A peptides as immunogens. In conclusion, we have successfully produced specific antibodies against LD-A. Moreover, our findings underscore the utility of bioinformatics tools for determining the optimal positions of immunizing peptides.

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Pipeline

Pipeline Snapshot as of 18 May 2025

The statistics for drugs in the Pipeline is the current organization and its subsidiaries are counted as organizations,Early Phase 1 is incorporated into Phase 1, Phase 1/2 is incorporated into phase 2, and phase 2/3 is incorporated into phase 3

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