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The LIM-domain-only protein LMO2 and its binding partner LDB1 are differentially required for class switch recombination.

Proc Natl Acad Sci U S A

January 2025

Department of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.

The LIM-domain-only protein LMO2 interacts with LDB1 in context-dependent multiprotein complexes and plays key roles in erythropoiesis and T cell leukemogenesis, but whether they have any roles in B cells is unclear. Through a CRISPR/Cas9-based loss-of-function screening, we identified LMO2 and LDB1 as factors for class switch recombination (CSR) in murine B cells. LMO2 contributes to CSR at least in part by promoting end joining of DNA double-strand breaks (DSBs) and inhibiting end resection.

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We describe a workshop that prompts chemistry students in the final 2 years of secondary school to apply their understanding of modern analytical chemistry techniques to a 'real world' example. The scenario used is that of a forensic science laboratory that has been asked to determine the structure of an illicit compound, Revisomed (methamphetamine) being sold as a revision aid, and seized by police. Over the course of an hour, the students use a combination of infrared (IR) spectroscopy, liquid chromatography (LC), high-resolution mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy data to determine the structure of Revisomed from first principles.

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The application of biological therapy and glucocorticoids in Auto-immune diseases (AID) patients will cause immunocompromised host (ICH) prone to infection. And monocytes play a key role in both innate and adaptive immune responses. We aimed to investigate the changes of circulating monocyte subsets in AID or AID-ICH patients with pulmonary infection.

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Classification and characteristics of bacterial glycosaminoglycan lyases, and their therapeutic and experimental applications.

J Cell Sci

January 2025

National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology and State Key Laboratory of Microbial Technology, Shandong University, 72 Binhai Rd, Qingdao, 266237, People's Republic of China.

Glycosaminoglycans (GAGs), as animal polysaccharides, are linked to proteins to form various types of proteoglycans. Bacterial GAG lyases are not only essential enzymes that spoilage bacteria use for the degradation of GAGs, but also valuable tools for investigating the biological function and potential therapeutic applications of GAGs. The ongoing discovery and characterization of novel GAG lyases has identified an increasing number of lyases suitable for functional studies and other applications involving GAGs, which include oligosaccharide sequencing, detection and removal of specific glycan chains, clinical drug development and the design of novel biomaterials and sensors, some of which have not yet been comprehensively summarized.

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Background Type I diabetes mellitus (T1DM) is a prevalent chronic illness that typically manifests in childhood. In patients who are genetically predisposed to diabetes, complex interactions between environmental and genetic factors play a role in the development of type 1 diabetes. There is proof that the onset of type 1 diabetes raises the possibility of developing additional autoimmune conditions.

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