دورية أكاديمية
أعرض في EDS

An X-Domain Phosphoinositide Phospholipase C (PI-PLC-like) of Trypanosoma brucei Has a Surface Localization and Is Essential for Proliferation.

التفاصيل البيبلوغرافية
العنوان: An X-Domain Phosphoinositide Phospholipase C (PI-PLC-like) of Trypanosoma brucei Has a Surface Localization and Is Essential for Proliferation.
المؤلفون: Negrão NW; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA.; Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA., Crowe LP; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA., Mantilla BS; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA.; Department of Biosciences, Durham University, Durham DHI 3LE, UK., Baptista RP; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA., King-Keller S; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA.; School of Science of Technology (Biology), Georgia Gwinnett College, Lawrenceville, GA 30043, USA., Huang G; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA., Docampo R; Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA.; Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA.
المصدر: Pathogens (Basel, Switzerland) [Pathogens] 2023 Feb 28; Vol. 12 (3). Date of Electronic Publication: 2023 Feb 28.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI AG Country of Publication: Switzerland NLM ID: 101596317 Publication Model: Electronic Cited Medium: Print ISSN: 2076-0817 (Print) Linking ISSN: 20760817 NLM ISO Abbreviation: Pathogens Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI AG, 2012-
مستخلص: Trypanosoma brucei is the causative agent of African trypanosomiasis, a deadly disease that affects humans and cattle. There are very few drugs to treat it, and there is evidence of mounting resistance, raising the need for new drug development. Here, we report the presence of a phosphoinositide phospholipase C (TbPI-PLC-like), containing an X and a PDZ domain, that is similar to the previously characterized TbPI-PLC1. TbPI-PLC-like only possesses the X catalytic domain and does not have the EF-hand, Y, and C2 domains, having instead a PDZ domain. Recombinant TbPI-PLC-like does not hydrolyze phosphatidylinositol 4,5-bisphosphate (PIP 2 ) and does not modulate TbPI-PLC1 activity in vitro. TbPI-PLC-like shows a plasma membrane and intracellular localization in permeabilized cells and a surface localization in non-permeabilized cells. Surprisingly, knockdown of TbPI-PLC-like expression by RNAi significantly affected proliferation of both procyclic and bloodstream trypomastigotes. This is in contrast with the lack of effect of downregulation of expression of TbPI-PLC1 .
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معلومات مُعتمدة: T32 AI060546 United States AI NIAID NIH HHS; AI077538 United States NH NIH HHS
فهرسة مساهمة: Keywords: Phospholipase C; RNA interference; Trypanosoma brucei; plasma membrane
تواريخ الأحداث: Date Created: 20230329 Latest Revision: 20230502
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC10051276
DOI: 10.3390/pathogens12030386
PMID: 36986308
قاعدة البيانات: MEDLINE
الوصف
تدمد:2076-0817
DOI:10.3390/pathogens12030386