BST2
- Known as:
- BST2
- Catalog number:
- 002692A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- BST2
Related genes to: BST2
- Gene:
- BST2 NIH gene
- Name:
- bone marrow stromal cell antigen 2
- Previous symbol:
- -
- Synonyms:
- CD317, tetherin
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-17
- Date modifiied:
- 2016-07-29
Related products to: BST2
Related articles to: BST2
- Artesunate is a worldwide prevalent antimalarial medicine, which has also been demonstrated for anti-tumor, anti-virus and anti-autoimmune diseases. Yet the underlying molecular and cellular mechanisms remain largely unexplored. Here, we examined immunological features of 5 immune tissues (spleen, bone marrow, thymus, lymph nodes and peritoneal cavity) of mice with artesunate administration through label-free proteomics and high-dimensional single-cell mass cytometry (CyTOF). Label-free proteomics uncovered dramatic alterations for the interferon-I (IFN-I) induced proteins, especially BST2 and IFIT1 downregulation in spleen and bone marrow. CyTOF analysis further indicated that the percentage of MDSCs was significantly elevated in spleen and bone marrow. The follow-up LPS-induced inflammatory model confirmed that pretreatment with artesunate attenuated the inflammatory damage, and the expression of BST2 was decreased in the spleen of mice with artesunate administration. Together, our findings presented an immune landscape of multiple tissues of mice with artesunate administration. These datasets provide comprehensive biological resources to develop therapeutic strategies for inflammatory diseases. - Source: PubMed
Publication date: 2026/04/12
Hong RongjianWang AitingLi YiyangDing Xianting - The HIV-1 envelope glycoprotein (Env) represents the only viral antigen at the surface of infected cells, making it an ideal target for antibody-based therapies. Most antibodies elicited in people with HIV (PWH) do not recognize Env in its native "closed" conformation but readily bind to Env when it samples the CD4-bound "open" conformation. Downregulation of CD4 at the surface of infected cells by the viral accessory proteins Nef and Vpu prevents the premature opening of Env and has been shown to protect infected cells from antibody-dependent cellular cytotoxicity (ADCC) mediated by PWH plasma. Here, we report that deletion of Nef and Vpu from primary infectious molecular clones renders infected cells vulnerable to antibody-dependent cellular phagocytosis (ADCP) mediated by PWH plasma. This is in part linked to the premature engagement of Env with CD4. In agreement with an "open" Env being vulnerable to ADCP, small CD4-mimetic compounds (CD4mc) sensitize -infected cells and -expanded CD4 T cells to ADCP mediated by autologous monocytes in the presence of PWH plasma. This effect was further improved by increasing cell surface Env through IFN-induced BST-2 upregulation.IMPORTANCEDeveloping new therapies to eliminate HIV-1-infected cells is essential to decrease the size of the HIV-1 reservoir. Fc-effector functions, such as antibody-dependent cellular cytotoxicity (ADCC), have shown potential in eliminating infected cells and expanded infected cells from people with HIV, decreasing the size of the reservoir, and delaying viral rebound in humanized mice. Here, we report that antibody-dependent cellular phagocytosis (ADCP) can also be harnessed to eliminate HIV-1-infected cells. We show that infected cells harboring "open" Env conformations are susceptible to ADCP-mediated killing in the presence of plasma from people with HIV. A better understanding of the contribution of different Fc-effector functions in the elimination of infected cells could help guide the development of new therapeutic approaches toward an HIV-1 cure. - Source: PubMed
Publication date: 2026/07/29
Bélanger ÉtienneTauzin AlexandraTajebe FitsumbrhanChandravanshi MonikaYang DerekChen Hung-ChingChiu Ta-JungBourassa CatherineMedjahed HalimaTolbert William DDurand MadeleineRichard JonathanHuryn Donna MStäger SimonaPazgier MarzenaFinzi Andrés - Multiple programmed cell death (PCD) modalities, including apoptosis, autophagy, and ferroptosis, are closely implicated in spontaneous preterm birth (SPTB). Mitochondria serve as central regulators of various PCD pathways, playing a critical role in cellular stress responses and homeostasis. However, comprehensive studies integrating mitochondria-localized protein-encoding genes and PCD-related genes to explore the molecular mechanisms underlying SPTB remain limited. - Source: PubMed
Publication date: 2026/07/20
Zuo LuguangHuai QingsongZhang MingmingLiu XinShang Xiaoling - Coordination between innate immune signaling and glucose metabolism is fundamental to organismal homeostasis, yet despite decades of study linking immunity and metabolism, the mechanisms by which metabolic cells restrain antiviral innate signaling while preserving glycolytic competence during overnutrition remain poorly defined. Here we identify Tetherin (BST2) as a unique cell-intrinsic immunometabolic checkpoint that couples restraint of type I interferon (IFN-I) signaling to preservation of glycolytic capacity in adipocytes. Tetherin localizes to endoplasmic reticulum and organizes an interactome enriched for antiviral sensing regulators and glycolytic control nodes in adipocytes. Mechanistically, Tetherin directly engages the ubiquitin-dependent degradation machinery NDFIP1 and RNF128 to terminate IRF3 activation, thereby limiting pro-inflammatory, anti-glycolytic signaling and protecting adipocytes from metabolic dysfunction. In parallel, multiomics integration reveals that Tetherin also acts as a scaffold that binds and spatially organizes and activates PFKFB3 to increase glycolytic capacity and restrain MAVS-IRF3 innate immune signalling. In vivo, adipocyte-specific loss of Tetherin amplifies high sucrose diet and high-fat-diet-induced glucose intolerance and liver steatosis, whereas overexpression of human Tetherin in adipocyte suppresses obesity-driven interferon signaling, restores glycolytic pathway, and improves metabolic homeostasis. Orthogonal perturbations in cancer and insulinoma cells further confirm an immunometabolic role for Tetherin. Together, these findings define Tetherin as a dual node immunometabolic checkpoint that couples restraint of antiviral innate inflammatory signaling to maintenance of glycolytic competence, thereby safeguarding adipocyte metabolic homeostasis. - Source: PubMed
Publication date: 2026/07/07
Cho Chung HwanJang YoungUkWarnock AidanYildiz RamazanJhang JingDavi KajalBrisnovali Niki FHuhn VictoriaWang PengBevaqua RominaGoedeke LeighSchotsaert Michael ABerisa MirelaPuleston DanielRajbhandari Prashant - Diatoms are major contributors to marine primary production and global CO2 fixation, with the centric diatom Thalassiosira pseudonana a powerful model for understanding biogeochemical processes including carbon fixation and silicification. Whilst there are molecular tools available for fluorescent protein (FP) tagging and CRISPR/Cas9 genome editing in T. pseudonana, these require the delivery of multiple vectors or have limited versatility. Additionally, scarless endogenous tagging, that results in a fluorescent protein fusion expressed from its native genomic location, has yet to be developed. Here we describe a versatile modular Golden Gate-based toolkit for T. pseudonana that through the delivery of a single-episome via bacterial conjugation enables: [1] FP tagging, [2] dual FP tagging, [3] CRISPR/Cas9 genome editing, [4] simultaneous FP tagging with gene editing, and [5] scarless endogenous FP tagging. We further expand the available parts for T. pseudonana by validating three additional FPs and two untested promoter/terminator pairs. We demonstrate the versatility of our system by knocking out Diatom Pyrenoid Component 1 (DPC1), whilst simultaneously GFP tagging the Rubisco small subunit (rbcS); and by endogenously GFP tagging the bestrophin-like protein BST2. Whilst DPC1 knock-out does not result in a major pyrenoid structural defect due to unperturbed rbcS-GFP localization to the pyrenoid, we confirm that BST2 localizes to the pyrenoid and exhibits increased fluorescence under low CO2 - supporting a role in diatom carbon fixation. Our developed genetic tools provide a robust framework for exploring cellular processes in diatoms, accelerating routine studies and enabling systematic, quantitative and large-scale studies. - Source: PubMed
Publication date: 2026/07/01
Nam OnyouGrouneva IrinaMackinder Luke C M