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2
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G protein signaling in the parasite Entamoeba histolytica.寄生虫溶组织内阿米巴中的 G 蛋白信号转导。
Exp Mol Med. 2013 Mar 22;45(3):e15. doi: 10.1038/emm.2013.30.
2
Heterotrimeric G-protein signaling is critical to pathogenic processes in Entamoeba histolytica.异三聚体 G 蛋白信号转导对于溶组织内阿米巴的致病过程至关重要。
PLoS Pathog. 2012;8(11):e1003040. doi: 10.1371/journal.ppat.1003040. Epub 2012 Nov 15.
3
Real-time analysis of gut flora in Entamoeba histolytica infected patients of Northern India.实时分析印度北部地区感染溶组织内阿米巴患者的肠道菌群。
BMC Microbiol. 2012 Aug 22;12:183. doi: 10.1186/1471-2180-12-183.
4
Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39.溶组织内阿米巴通过跨膜激酶 39 部分调控的受体介导摄取大肠杆菌和 LDL 胆固醇的共同途径。
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The repertoire of G protein-coupled receptors in the human parasite Schistosoma mansoni and the model organism Schmidtea mediterranea.人源寄生虫曼氏血吸虫和模式生物地中海扁虫中的 G 蛋白偶联受体谱。
BMC Genomics. 2011 Dec 6;12:596. doi: 10.1186/1471-2164-12-596.
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Brain angiogenesis inhibitor 1 (BAI1) is a pattern recognition receptor that mediates macrophage binding and engulfment of Gram-negative bacteria.脑血管生成抑制剂 1(BAI1)是一种模式识别受体,可介导巨噬细胞结合并吞噬革兰氏阴性菌。
Proc Natl Acad Sci U S A. 2011 Feb 1;108(5):2136-41. doi: 10.1073/pnas.1014775108. Epub 2011 Jan 18.
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Identification of an Ascaris G protein-coupled acetylcholine receptor with atypical muscarinic pharmacology.鉴定一种具有非典型毒蕈碱药理学的蛔虫 G 蛋白偶联乙酰胆碱受体。
Int J Parasitol. 2009 Sep;39(11):1215-22. doi: 10.1016/j.ijpara.2009.03.001. Epub 2009 Mar 25.
8
Short hairpin RNA-mediated knockdown of protein expression in Entamoeba histolytica.短发夹RNA介导的溶组织内阿米巴蛋白表达敲低
BMC Microbiol. 2009 Feb 17;9:38. doi: 10.1186/1471-2180-9-38.
9
The interplay between Entamoeba and enteropathogenic bacteria modulates epithelial cell damage.内阿米巴与肠道致病菌的相互作用可调节上皮细胞损伤。
PLoS Negl Trop Dis. 2008 Jul 23;2(7):e266. doi: 10.1371/journal.pntd.0000266.
10
Entamoeba histolytica phagocytosis of human erythrocytes involves PATMK, a member of the transmembrane kinase family.溶组织内阿米巴对人类红细胞的吞噬作用涉及跨膜激酶家族成员PATMK。
PLoS Pathog. 2008 Jan;4(1):e8. doi: 10.1371/journal.ppat.0040008.

溶组织内阿米巴吞噬细菌过程中存在识别细菌脂多糖的G蛋白偶联受体的证据。

Evidence for a bacterial lipopolysaccharide-recognizing G-protein-coupled receptor in the bacterial engulfment by Entamoeba histolytica.

作者信息

Brewer Matthew T, Agbedanu Prince N, Zamanian Mostafa, Day Tim A, Carlson Steve A

机构信息

Department of Biomedical Sciences, College of Veterinary Medicine, Iowa State University, Ames, Iowa, USA.

出版信息

Eukaryot Cell. 2013 Nov;12(11):1433-8. doi: 10.1128/EC.00150-13. Epub 2013 Aug 23.

DOI:10.1128/EC.00150-13
PMID:23975887
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3837928/
Abstract

Entamoeba histolytica is the causative agent of amoebic dysentery, a worldwide protozoal disease that results in approximately 100,000 deaths annually. The virulence of E. histolytica may be due to interactions with the host bacterial flora, whereby trophozoites engulf colonic bacteria as a nutrient source. The engulfment process depends on trophozoite recognition of bacterial epitopes that activate phagocytosis pathways. E. histolytica GPCR-1 (EhGPCR-1) was previously recognized as a putative G-protein-coupled receptor (GPCR) used by Entamoeba histolytica during phagocytosis. In the present study, we attempted to characterize EhGPCR-1 by using heterologous GPCR expression in Saccharomyces cerevisiae. We discovered that bacterial lipopolysaccharide (LPS) is an activator of EhGPCR-1 and that LPS stimulates EhGPCR-1 in a concentration-dependent manner. Additionally, we demonstrated that Entamoeba histolytica prefers to engulf bacteria with intact LPS and that this engulfment process is sensitive to suramin, which prevents the interactions of GPCRs and G-proteins. Thus, EhGPCR-1 is an LPS-recognizing GPCR that is a potential drug target for treatment of amoebiasis, especially considering the well-established drug targeting to GPCRs.

摘要

溶组织内阿米巴是阿米巴痢疾的病原体,这是一种全球范围内的原生动物疾病,每年导致约10万例死亡。溶组织内阿米巴的毒力可能归因于与宿主细菌菌群的相互作用,即滋养体将结肠细菌作为营养源吞噬。吞噬过程取决于滋养体对激活吞噬途径的细菌表位的识别。溶组织内阿米巴GPCR-1(EhGPCR-1)先前被认为是溶组织内阿米巴在吞噬过程中使用的一种假定的G蛋白偶联受体(GPCR)。在本研究中,我们试图通过在酿酒酵母中进行异源GPCR表达来表征EhGPCR-1。我们发现细菌脂多糖(LPS)是EhGPCR-1的激活剂,并且LPS以浓度依赖的方式刺激EhGPCR-1。此外,我们证明溶组织内阿米巴更喜欢吞噬具有完整LPS的细菌,并且这种吞噬过程对苏拉明敏感,苏拉明可阻止GPCR与G蛋白的相互作用。因此,EhGPCR-1是一种识别LPS的GPCR,是治疗阿米巴病的潜在药物靶点,特别是考虑到针对GPCR的药物已得到充分确立。