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THE JOURNAL OF BIOLOGICAL CHEMISTRY: The Biochemical Behavior of LeadL I. Influence of Calcium, Phosphorus, and Vitamin D on Lead in Blood and Bone

K. JAMES: Anti-lymphocytic antibody--A review B. L. DINH & A. BRASSARD: Induction of experimental glomerulonephritis in the rat by homologous major urinary protein J. R. HOBBS & MARGARET TURNER-WARWICK: Assay of circulating immunoglobulins in patients with fibrosing alveolitis KATHLEEN HAYES, J. A. DUDGEON & J. F. SOOTHILL: Humoral immunity in congenital rubella I. P. T. H ~ K K I N E N & S. VIRTANEN: The blood group activity of human gastric sulphogtycoproteins in patients with gastric cancer and normal controls C. A. RAMSEY & G. L. ASHERSON: A human serum factor (antibody) against altered human serum albumin K. JAMES: Some factors influencing the ability of anti-lymphocytic antibody to suppress humoral antibody formation C. BRAUTBAR & D. NELKEN: Accelerated rejection of rat allografts after the rejection of rabbit skin grafts ANNI H~rHN & R. C. NAIRN: A nuclear staining artefact in immunofluorescence

Clinical and Experimental Immunology

Pyroptosis, an inflammatory form of programmed cell death, has been implicated in eliminating pathogenic infections. However, macrophage pyroptosis–related proteins from Mycobacterium tuberculosis (M.tb) have largely gone unexplored. Here, we identified a cell pyroptosis–inducing protein, Rv1579c, named EST12, secreted from the M.tb H37Rv region of difference 3. EST12 binds to the receptor for activated C kinase 1 (RACK1) in macrophages, and the EST12-RACK1 complex recruits the deubiquitinase UCHL5 to promote the K48-linked deubiquitination of NLRP3, subsequently leading to an NLRP3 inflammasome caspase-1/11–pyroptosis gasdermin D–interleukin-1β immune process. Analysis of the crystal structure of EST12 reveals that the amino acid Y80 acts as a critical binding site for RACK1. An EST12-deficient strain (H37RvΔEST12) displayed higher susceptibility to M.tb infection in vitro and in vivo. These results provide the first proof that RACK1 acts as an endogenous host sensor for pathogens and that EST12-RACK1–induced pyroptosis plays a pivotal role in M.tb-induced immunity.

https://advances.sciencemag.org/content/advances/6/43/eaba4733.full.pdf

Mycobacterial EST12 activates a RACK1-NLRP3-gasdermin D pyroptosis-IL-1β immune pathway.

Oligonucleotide aptamers: promising and powerful diagnostic and therapeutic tools for infectious diseases.

Mycobacterium tuberculosis Mannose-Capped Lipoarabinomannan Induces IL-10-Producing B Cells and Hinders CD4+Th1 Immunity.

Because Mycobacterium bovis, termed bacillus Calmette–Guerin (BCG), the only available used tuberculosis (TB) vaccine, retains immunomodulatory properties that limit its protective immunogenicity, there are continuous efforts to identify the immunosuppression mechanism as well as new strategies for improving the immunogenicity of BCG. Here, an ssDNA aptamer “antibody” BM2 specifically bound to the mannose-capped lipoarabinomannan (ManLAM) of BCG was selected. BM2 significantly blocked ManLAM–mannose receptor (MR) binding, triggered ManLAM–CD44 signaling, and enhanced M1 macrophage and Th1 activation via cellular surface CD44 in vitro and in vivo. BM2 enhanced immunoprotective effects of BCG against virulent Mycobacterium tuberculosis H37Rv infection in mice and monkeys models. Thus, we report a new mechanism of the interaction between ManLAM and CD44 on macrophages and CD4+ T cells and reveal that ManLAM-binding membrane molecule CD44 is a novel target for the enhancement of BCG immunogenicity, and BM2 ha...

A Single ssDNA Aptamer Binding to Mannose-Capped Lipoarabinomannan of Bacillus Calmette–Guérin Enhances Immunoprotective Effect against Tuberculosis

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A Single ssDNA Aptamer Binding to Mannose-Capped Lipoarabinomannan of Bacillus Calmette–Guérin Enhances Immunoprotective Effect against Tuberculosis