SDS-PAGE showing purified DAG protein (indicated by arrow).

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ALPHA-DYSTROGLYCAN (DAG) – RECOMBINANT PROTEIN
Recombinant human alpha-dystroglycan (DAG) protein produced in HEK293 cells. DAG is a major cellular receptor for Lassa Fever virus (LAFV).
PRODUCT DETAILS – ALPHA-DYSTROGLYCAN (DAG) – RECOMBINANT PROTEIN
- Recombinant human alpha-dystroglycan (DAG) – NCBI accession number NP_004384.4, amino acids 28-651.
- C-terminal transmembrane domain and the cytoplasmic tail replaced by 15 aa Glycine-Serine linker and human IgG1 Fc-tag.
- Produced in HEK293 cells and purified from culture supernatant.
- Stored in PBS, pH7.4.
BACKGROUND
The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Lassa fever virus (LAFV) exhibits broad tissue tropism and its major cellular receptor is extracellular matrix receptor dystroglycan (DG). DG is a ubiquitously expressed and highly conserved receptor for extracellular matrix (ECM) proteins, where it provides a molecular link between the ECM and the actin-based cytoskeleton (Cao et al., 1998). DG is cleaved into the extracellular alpha-DG (α-DG) and membrane-anchored β-DG (Barresi and Campbell, 2006). In mammals, α-DG is also subject to complex O-glycosylation, which is essential for its function as a receptor for ECM proteins and arenaviruses (Yoshida-Moriguchi and Campbell, 2015; Kunz et al., 2005; Rojek et al., 2007). Binding of LASV depends on DG’s tissue-specific posttranslational modification with the unusual O-linked polysaccharide matriglycan. However, functional glycosylation of DG does not always correlate with viral tropism observed in vivo, suggesting the existence of alternative receptors. The broadly expressed phosphatidylserine (PS) receptors Axl and Tyro3 have also been identified as alternative LASV receptor candidates (Fedeli et al., 2018).
Alpha-dystroglycan also acts as a receptor for lymphocytic choriomeningitis virus glycoprotein and class C new-world arenaviruses (Imperiali et al., 2005, Kunz, 2009; Rojek et al., 2007). It is also the Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2 (Rambukkana et al., 2008).
REFERENCES
- Barresi and Campbell (2006). Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci. 119(Pt 2):199-207.
- Cao et al. (1998). Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus. Science. 282(5396):2079-81.
- Fedeli et al. (2018). Axl Can Serve as Entry Factor for Lassa Virus Depending on the Functional Glycosylation of Dystroglycan. J Virol. 92(5).
- Imperiali et al. (2005). O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function. J Virol. 79(22):14297-308.
- Kunz (2009). Receptor binding and cell entry of Old World arenaviruses reveal novel aspects of virus-host interaction. Virology. 387(2):245-9.
- Kunz et al. (2005). Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding. J Virol. 79(22):14282-96.
- Rojek et al. (2007). Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan’s host-derived ligands. J Virol. 81(11):5685-95.
- Rambukkana et al. (1998). Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae. Science. 282(5396):2076-9.
- Yoshida-Moriguchi and Campbell (2015). Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane. Glycobiology. 25(7):702-13.
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所以说,感染同一种病毒,每个人识别的表位可能不一样。
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2、抗原,是指能够刺激机体产生(特异性)免疫应答,并能与免疫应答产物抗体和致敏淋巴细胞在体外结合,发生免疫效应(特异性反应)的物质
核心抗原由183个或185个氨基酸组成,高度磷酸化,是乙肝病毒核心颗粒的唯一结构蛋白。正由于它存在于Dane颗粒核心结构表面,被表面抗原覆盖,故不易在血循环中检出。核心抗原具有强免疫原性,可诱导很强的体液免疫和细胞免疫,刺激机体产生抗-HBc。
e抗原为可溶性蛋白质,传染性强,游离存在于血液中,虽然很早就被发现,在病理上认为是HBV复制以具有强感染性的一个指标,但其功能尚不清楚。抗-HBe的出现,是预后良好的征象。向左转|向右转
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主要是中度以上细胞免疫缺陷包括:CD4+T淋巴细胞耗竭,外周血淋巴细胞显著减少,CD4<200/μl,CD4/CD8<1.0,(正常人为1.25~2.1),迟发型变态反应皮试阴性,有丝分裂原刺激反应低下。NK细胞活性下降。
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