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Rab7 controls lipid droplet-phagosome association during mycobacterial infection.
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids ( IF 3.9 ) Pub Date : 2020-03-27 , DOI: 10.1016/j.bbalip.2020.158703 Natalia R Roque 1 , Silvia L Lage 1 , Roberta Navarro 1 , Narayana Fazolini 1 , Clarissa M Maya-Monteiro 1 , Jens Rietdorf 2 , Rossana C N Melo 3 , Heloisa D'Avila 3 , Patricia T Bozza 1
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids ( IF 3.9 ) Pub Date : 2020-03-27 , DOI: 10.1016/j.bbalip.2020.158703 Natalia R Roque 1 , Silvia L Lage 1 , Roberta Navarro 1 , Narayana Fazolini 1 , Clarissa M Maya-Monteiro 1 , Jens Rietdorf 2 , Rossana C N Melo 3 , Heloisa D'Avila 3 , Patricia T Bozza 1
Affiliation
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Lipid droplets (LDs) are organelles that have multiple roles in inflammatory and infectious diseases. LD act as essential platforms for immunometabolic regulation, including as sites for lipid storage and metabolism, inflammatory lipid mediator production, and signaling pathway compartmentalization. Accumulating evidence indicates that intracellular pathogens may exploit host LDs as source of nutrients and as part of their strategy to promote immune evasion. Notably, numerous studies have demonstrated the interaction between LDs and pathogen-containing phagosomes. However, the mechanism involved in this phenomenon remains elusive. Here, we observed LDs and PLIN2 surrounding M. bovis BCG-containing phagosomes, which included observations of a bacillus cell surrounded by lipid content inside a phagosome and LAM from mycobacteria co-localizing with LDs; these results were suggestive of exchange of contents between these compartments. By using beads coated with M.tb lipids, we demonstrated that LD-phagosome associations are regulated through the mycobacterial cell wall components LAM and PIM. In addition, we demonstrated that Rab7 and RILP, but not Rab5, localizes to LDs of infected macrophages and observed the presence of Rab7 at the site of interaction with an infected phagosome. Moreover, treatment of macrophages with the Rab7 inhibitor CID1067700 significantly inhibited the association between LDs and LAM-coated beads. Altogether, our data demonstrate that LD-phagosome interactions are controlled by mycobacterial cell wall components and Rab7, which enables the exchange of contents between LDs and phagosomes and may represent a fundamental aspect of bacterial pathogenesis and immune evasion.
中文翻译：
Rab7在分枝杆菌感染过程中控制脂质滴与吞噬体的结合。
脂质滴（LDs）是在炎症和传染病中具有多种作用的细胞器。LD充当免疫代谢调节的重要平台，包括脂质存储和代谢，炎性脂质介导物产生以及信号通路分隔的位点。越来越多的证据表明，细胞内病原体可能利用宿主LDs作为营养物质来源，并作为其促进免疫逃逸策略的一部分。值得注意的是，大量研究证明了LD与含病原体的吞噬体之间的相互作用。但是，这种现象所涉及的机制仍然难以捉摸。在这里，我们观察到了含有牛分枝杆菌BCG吞噬体的LD和PLIN2，其中包括观察到细菌细胞被分枝杆菌与LDs共定位的吞噬体和LAM中的脂质含量所包围；这些结果表明这些隔室之间的内容物交换。通过使用涂有M.tb脂质的珠子，我们证明了LD-吞噬体的结合是通过分枝杆菌细胞壁成分LAM和PIM来调节的。此外，我们证明了Rab7和RILP，而不是Rab5，位于感染的巨噬细胞的LDs处，并观察到Rab7在与感染的吞噬体相互作用的位点。此外，用Rab7抑制剂CID1067700处理巨噬细胞可显着抑制LD与LAM包被的磁珠之间的缔合。总体而言，我们的数据表明LD-吞噬体相互作用受分枝杆菌细胞壁成分和Rab7的控制，
更新日期：2020-03-27
中文翻译：
Rab7在分枝杆菌感染过程中控制脂质滴与吞噬体的结合。
脂质滴（LDs）是在炎症和传染病中具有多种作用的细胞器。LD充当免疫代谢调节的重要平台，包括脂质存储和代谢，炎性脂质介导物产生以及信号通路分隔的位点。越来越多的证据表明，细胞内病原体可能利用宿主LDs作为营养物质来源，并作为其促进免疫逃逸策略的一部分。值得注意的是，大量研究证明了LD与含病原体的吞噬体之间的相互作用。但是，这种现象所涉及的机制仍然难以捉摸。在这里，我们观察到了含有牛分枝杆菌BCG吞噬体的LD和PLIN2，其中包括观察到细菌细胞被分枝杆菌与LDs共定位的吞噬体和LAM中的脂质含量所包围；这些结果表明这些隔室之间的内容物交换。通过使用涂有M.tb脂质的珠子，我们证明了LD-吞噬体的结合是通过分枝杆菌细胞壁成分LAM和PIM来调节的。此外，我们证明了Rab7和RILP，而不是Rab5，位于感染的巨噬细胞的LDs处，并观察到Rab7在与感染的吞噬体相互作用的位点。此外，用Rab7抑制剂CID1067700处理巨噬细胞可显着抑制LD与LAM包被的磁珠之间的缔合。总体而言，我们的数据表明LD-吞噬体相互作用受分枝杆菌细胞壁成分和Rab7的控制，
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