Rab蛋白参与结核分枝杆菌胞内吞噬的研究进展

doi:10.16352/j.issn.1001-6325.2022.10.1596

基础医学与临床 ›› 2022, Vol. 42 ›› Issue (10): 1596-1600.doi: 10.16352/j.issn.1001-6325.2022.10.1596

Rab蛋白参与结核分枝杆菌胞内吞噬的研究进展

孙巧玲, 袁欣, 秦欢, 王玉^*

遵义医科大学基础医学院微生物学教研室, 贵州遵义 563003

收稿日期:2021-07-16 修回日期:2021-11-12 出版日期:2022-10-05 发布日期:2022-09-23
通讯作者: * anguwy@126.com
基金资助:
贵州省科技计划项目([2018]1191);遵义医科大学博士科研启动基金(F-810)

Research advances on Rab protein involved in intracellular phagocytosis of Mycobacterium tuberculosis

SUN Qiao-ling, YUAN Xin, QIN Huan, WANG Yu^*

Department of Microbiology, College of Basic Medicine, Zunyi Medical University, Zunyi 563003, China

Received:2021-07-16 Revised:2021-11-12 Online:2022-10-05 Published:2022-09-23
Contact: * anguwy@126.com

摘要/Abstract

摘要： 结核分枝杆菌(Mtb)是结核病的病原体,可通过调控细胞吞噬作用来促进胞内细菌的存活,并干扰宿主细胞的生理功能。Rab蛋白是胞内膜转运过程的重要组分,参与和调节了Mtb的吞噬过程。本文主要介绍Mtb及其菌体成分对胞内吞噬的影响,并就Rab蛋白在其中的作用进行论述,从而探讨Rab蛋白与Mtb胞内吞噬的关系,为进一步研究Mtb胞内免疫机制提供理论基础。

关键词: 结核分枝杆菌, 菌体成分, Rab蛋白, 吞噬

Abstract: Mycobacterium tuberculosis(M.tuberculosis, Mtb)is the causative agent of tuberculosis and can survive through regulating intracellular phagocytosis and affect the biological function of host cells. Rab proteins are important components of intracellular membrane transport and involved in the phagocytosis of Mtb. This review summarized the effect of Mtb and its compositions on intracellular phagocytosis and the role of Rab in this process. Thus this review may provide some ideas to understand the relationship between Rab proteins and the phagocytosis of Mtb, and to provide new thoughts and potential targets based on exploring the intracellular immune mechanism of Mtb.

Key words: Mycobacterium tuberculosis, bacterium components, Rab protein, phagocytosis

中图分类号:

R378.91

孙巧玲, 袁欣, 秦欢, 王玉. Rab蛋白参与结核分枝杆菌胞内吞噬的研究进展[J]. 基础医学与临床, 2022, 42(10): 1596-1600.

SUN Qiao-ling, YUAN Xin, QIN Huan, WANG Yu. Research advances on Rab protein involved in intracellular phagocytosis of Mycobacterium tuberculosis[J]. Basic & Clinical Medicine, 2022, 42(10): 1596-1600.

参考文献 26

[1]	World Health Organization. Global tuberculosis report 2020[M]. Geneva:World Health Organization, 2020:1-4.
[2]	Pidwill GR, Gibson JF, Cole J, et al. The role of macrophages in staphylococcus aureus infection[J]. Front Immunol, 2020, 11: 620339. doi: 10.3389/fimmu.2020.620339.
[3]	Simeone R, Sayes F, Lawaree E, et al. Breaching the phagosome, the case of the tuberculosis agent[J]. Cell Microbiol, 2021, 23: e13344. doi: 10.1111/cmi.13344.
[4]	Nakayama H, Kurihara H, Morita YS, et al. Lipoarabinomannan binding to lactosylceramide in lipid rafts is essential for the phagocytosis of mycobacteria by human neutrophils[J]. Sci Signal, 2016, 9: ra101. doi: 10.1126/scisignal.aaf1585.
[5]	Vazquez CL, Bianco MV, Blanco FC, et al. Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages[J]. Infect Immun, 2017, 85. doi: 10.1128/IAI.00720-16.
[6]	Osman MM, Pagan AJ, Shanahan JK, et al. Mycobacterium marinum phthiocerol dimycocerosates enhance macrophage phagosomal permeabilization and membrane damage[J]. PLoS One, 2020, 15: e0233252. doi: 10.1371/journal.pone.0233252.
[7]	Wang J, Ge P, Lei Z, et al. Mycobacterium tuberculosis protein kinase G acts as an unusual ubiquitinating enzyme to impair host immunity[J]. EMBO Rep, 2021, 22: e52175. doi: 10.15252/embr.202052175.
[8]	Wong D, Li W, Chao JD, et al. Protein tyrosine kinase, PtkA, is required for Mycobacterium tuberculosis growth in macrophages[J]. Sci Rep, 2018, 8: 155. doi: 10.1038/s41598-017-18547-9.
[9]	Singh KS, Sharma R, Keshari D, et al. Down-regulation of malate synthase in Mycobacterium tuberculosis H37Ra leads to reduced stress tolerance, persistence and survival in macrophages[J]. Tuberculosis (Edinb), 2017, 106: 73-81.
[10]	Sheffield DA, Jepsen MR, Feeney SJ, et al. The myotubularin MTMR4 regulates phagosomal phosphatidylinositol 3-phosphate turnover and phagocytosis[J]. J Biol Chem, 2019, 294: 16684-16697.
[11]	Koliwer-Brandl H, Knobloch P, Barisch C, et al. Distinct Mycobacterium marinum phosphatases determine pathogen vacuole phosphoinositide pattern, phagosome maturation, and escape to the cytosol[J]. Cell Microbiol, 2019, 21: e13008. doi: 10.1111/cmi.13008.
[12]	Cui Z, Dang G, Song N, et al. Rv3091, An extracellular patatin-like phospholipase in Mycobacterium tuberculosis, prolongs intracellular survival of recombinant Mycolicibacterium smegmatis by mediating phagosomal escape[J]. Front Microbiol, 2020, 11: 2204. doi: 10.3389/fmicb.2020.532371.
[13]	Jia L, Sha S, Yang S, et al. Effect of protein O-mannosyltransferase (MSMEG_5447) on M. smegmatis and its survival in macrophages[J]. Front Microbiol, 2021, 12: 657726. doi: 10.3389/fmicb.2021.657726.
[14]	Mehta M, Singh A. Mycobacterium tuberculosis WhiB3 maintains redox homeostasis and survival in response to reactive oxygen and nitrogen species[J]. Free Radic Biol Med, 2019, 131: 50-58.
[15]	Park HS, Back YW, Shin KW, et al. Mycobacterium tuberculosis Rv3463 induces Mycobactericidal activity in macrophages by enhancing phagolysosomal fusion and exhibits therapeutic potential[J]. Sci Rep, 2019, 9: 4246. doi: 10.1038/s41598-019-38982-0.
[16]	Lienard J, Nobs E, Lovins V, et al. The Mycobacterium marinum ESX-1 system mediates phagosomal permeabilization and type Ⅰ interferon production via separable mechanisms[J]. Proc Natl Acad Sci U S A, 2020, 117: 1160-1166.
[17]	Yabaji SM, Dhamija E, Mishra AK, et al. ESAT-6 regulates autophagous response through SOD-2 and as a result induces intracellular survival of Mycobacterium bovis BCG[J]. Biochim Biophys Acta Proteins Proteom, 2020, 1868: 140470. doi: 10.1016/j.bbapap.2020.140470.
[18]	Li F, Luo J, Xu H, et al. Early secreted antigenic target 6-kDa from Mycobacterium tuberculosis enhanced the protective innate immunity of macrophages partially via HIF1 alpha[J]. Biochem Biophys Res Commun, 2020, 522: 26-32.
[19]	Zuo X, Wang L, Bao Y, et al. The ESX-1 virulence factors downregulate miR-147-3p in Mycobacterium marinum-infected macrophages[J]. Infect Immun, 2020, 88: e00088-20. doi: 10.1128/IAI.00088-20.
[20]	Sun J, Deghmane AE, Soualhine H, et al. Mycobac-terium bovis BCG disrupts the interaction of Rab7 with RILP contributing to inhibition of phagosome maturation[J]. J Leukoc Biol, 2007, 82: 1437-1445.
[21]	Roque NR, Lage SL, Navarro R, et al. Rab7 controls lipid droplet-phagosome association during mycobacterial infection[J]. Biochim Biophys Acta: Mol Cell Biol Lipids, 2020, 1865: 158703. doi: 10.1016/j.bbalip.2020.158703.
[22]	Cardoso CM, Jordao L, Vieira OV. Rab10 regulates phagosome maturation and its overexpression rescues Mycobacterium-containing phagosomes maturation[J]. Traffic, 2010, 11: 221-235.
[23]	Zhu Y, Xiao Y, Kong D, et al. Down-regulation of miR-378d increased Rab10 expression to help clearance of Mycobacterium tuberculosis in macrophages[J]. Front Cell Infect Microbiol, 2020, 10: 108. doi: 10.3389/fcimb.2020.00108.
[24]	Kyei GB, Vergne I, Chua J, et al. Rab14 is critical for maintenance of Mycobacterium tuberculosis phagosome maturation arrest[J]. EMBO J, 2006, 25: 5250-5259.
[25]	Segawa T, Hazeki K, Nigorikawa K, et al. Inpp5e increases the Rab5 association and phosphatidylinositol 3-phosphate accumulation at the phagosome through an interac-tion with Rab20[J]. Biochem J, 2014, 464: 365-375.
[26]	Pradhan G, Shrivastva R, Mukhopadhyay S. Mycobacterial PknG targets the Rab7l1 signaling pathway to inhibit phagosome-lysosome fusion[J]. J Immunol, 2018, 201: 1421-1433.

Rab蛋白参与结核分枝杆菌胞内吞噬的研究进展

Research advances on Rab protein involved in intracellular phagocytosis of Mycobacterium tuberculosis

PDF

可视化

摘要/Abstract

引用本文

使用本文

参考文献 26

相关文章 7

编辑推荐

Metrics

本文评价

[1]	秦晓莉, 赵琳娜, 付榕, 郭玉莹, 徐士欣. 星形胶质细胞吞噬作用在阿尔茨海默病中的研究进展[J]. 基础医学与临床, 2024, 44(8): 1180-1184.
[2]	陈笑天, 陈翀, 罗云萍. MAFB对肿瘤相关巨噬细胞极化及功能的影响[J]. 基础医学与临床, 2024, 44(7): 965-973.
[3]	薛雨佳, 李子坚. 细胞内凝血因子ⅩⅢ研究进展[J]. 基础医学与临床, 2021, 41(11): 1680-1683.
[4]	姬文兰王启源. Annexin 1抑制BCG诱导的巨噬细胞RAW246.7细胞炎性应答及凋亡[J]. 基础医学与临床, 2018, 38(8): 1121-1126.
[5]	李金阳姚剑挺盛思琪田野王丽娜. 细胞凋亡和有效吞噬在动脉粥样硬化斑块中的作用[J]. 基础医学与临床, 2018, 38(4): 548-552.
[6]	胡继芬何芳杰陈丽红吴建波. 血栓素受体参与子痫前期的发病[J]. 基础医学与临床, 2015, 35(7): 921-924.
[7]	甘辛陈玲王建华李娜娜陈杨张建勇张泓. 结核分枝杆菌耐利福平rpoB基因突变的序列分析[J]. 基础医学与临床, 2010, 30(3): 268-271.