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Review Article | Open Access

The regulation of host cytoskeleton during SARS-CoV-2 infection in the nervous system

Unit of Cell Biology and Imaging Study of Pathogen Host Interaction, The Center for Microbes, Development and Health, CAS Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai 200031, China
University of Chinese Academy of Sciences, Beijing 100049, China
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Abstract

The global economy and public health are currently under enormous pressure since the outbreak of COVID-19. Apart from respiratory discomfort, a subpopulation of COVID-19 patients exhibits neurological symptoms such as headache, myalgia, and loss of smell. Some have even shown encephalitis and necrotizing hemorrhagic encephalopathy. The cytoskeleton of nerve cells changes drastically in these pathologies, indicating that the cytoskeleton and its related proteins are closely related to the pathogenesis of nervous system diseases. In this review, we present the up-to-date association between host cytoskeleton and coronavirus infection in the context of the nervous system. We systematically summarize cytoskeleton-related pathogen-host interactions in both the peripheral and central nervous systems, hoping to contribute to the development of clinical treatment in COVID-19 patients.

References

[1]
Shi XM, Fan CY, Jiu YM. Unidirectional regulation of vimentin intermediate filaments to caveolin-1. Int J Mol Sci 2020, 21(20): 7436.
[2]
Wang JY, Zhang W, Roehrl MW, et al. An autoantigen profile of human A549 lung cells reveals viral and host etiologic molecular attributes of autoimmunity in COVID-19. J Autoimmun 2021, 120: 102644.
[3]
Helfand BT, Mendez MG, Murthy SNP, et al. Vimentin organization modulates the formation of lamellipodia. MBoC 2011, 22(8): 1274–1289.
[4]
Cheever TR, Ervasti JM. Actin isoforms in neuronal development and function. Int Rev Cell Mol Biol 2013, 301: 157–213.
[5]
Zandi F, Khalaj V, Goshadrou F, et al. Rabies virus matrix protein targets host actin cytoskeleton: a protein-protein interaction analysis. Pathog Dis 2021, 79(1): ftaa075.
[6]
Jhan MK, Tsai TT, Chen CL, et al. Dengue virus infection increases microglial cell migration. Sci Rep 2017, 7(1): 91.
[7]
Zhao SS, Gao JK, Zhu LQ, et al. Transmissible gastroenteritis virus and porcine epidemic diarrhoea virus infection induces dramatic changes in the tight junctions and microfilaments of polarized IPEC-J2 cells. Virus Res 2014, 192: 34–45.
[8]
Janke C, Kneussel M. Tubulin post-translational modifications: encoding functions on the neuronal microtubule cytoskeleton. Trends Neurosci 2010, 33(8): 362–372.
[9]
Xiao QP, Hu XH, Wei ZY, et al. Cytoskeleton molecular motors: structures and their functions in neuron. Int J Biol Sci 2016, 12(9): 1083–1092.
[10]
Trushina NI, Mulkidjanian AY, Brandt R. The microtubule skeleton and the evolution of neuronal complexity in vertebrates. Biol Chem 2019, 400(9): 1163–1179.
[11]
Hahn I, Voelzmann A, Liew YT, et al. The model of local axon homeostasis - explaining the role and regulation of microtubule bundles in axon maintenance and pathology. Neural Dev 2019, 14(1): 11.
[12]
Baas PW, Rao AN, Matamoros AJ, et al. Stability properties of neuronal microtubules. Cytoskeleton (Hoboken) 2016, 73(9): 442–460.
[13]
Sodeik B, Ebersold MW, Helenius A. Microtubule-mediated transport of incoming Herpes simplex virus 1 capsids to the nucleus. J Cell Biol 1997, 136(5): 1007–1021.
[14]
Suomalainen M, Nakano MY, Keller S, et al. Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J Cell Biol 1999, 144(4): 657–672.
[15]
Suikkanen S, Aaltonen T, Nevalainen M, et al. Exploitation of microtubule cytoskeleton and dynein during parvoviral traffic toward the nucleus. J Virol 2003, 77(19): 10270–10279.
[16]
Wang IH, Burckhardt CJ, Yakimovich A, et al. Imaging, tracking and computational analyses of virus entry and egress with the cytoskeleton. Viruses 2018, 10(4): 166.
[17]
Yuan AD, Rao MV, Veeranna, et al. Neurofilaments and neurofilament proteins in health and disease. Cold Spring Harb Perspect Biol 2017, 9(4): a018309.
[18]
Yang LF, Tang L, Dai F, et al. Raf-1/CK2 and RhoA/ROCK signaling promote TNF-α-mediated endothelial apoptosis via regulating vimentin cytoskeleton. Toxicology 2017, 389: 74–84.
[19]
Ehrenreiter K, Piazzolla D, Velamoor V, et al. Raf-1 regulates Rho signaling and cell migration. J Cell Biol 2005, 168(6): 955–964.
[20]
Larsson C. Protein kinase C and the regulation of the actin cytoskeleton. Cell Signal 2006, 18(3): 276–284.
[21]
Galigniana NM, Charó NL, Uranga R, et al. Oxidative stress induces transcription of telomeric repeat-containing RNA (TERRA) by engaging PKA signaling and cytoskeleton dynamics. Biochim Biophys Acta BBA Mol Cell Res 2020, 1867(4): 118643.
[22]
Benoit B, Baillet A, Poüs C. Cytoskeleton and associated proteins: pleiotropic JNK substrates and regulators. Int J Mol Sci 2021, 22(16): 8375.
[23]
Choong G, Liu Y, Templeton DM. Cadmium affects focal adhesion kinase (FAK) in mesangial cells: involvement of CaMK-II and the actin cytoskeleton. J Cell Biochem 2013, 114(8): 1832–1842.
[24]
Beziau A, Brand D, Piver E. The role of phosphatidylinositol phosphate kinases during viral infection. Viruses 2020, 12(10): 1124.
[25]
Dunn CW, Hejnol A, Matus DQ, et al. Broad phylogenomic sampling improves resolution of the animal tree of life. Nature 2008, 452(7188): 745–749.
[26]
Netland J, Meyerholz DK, Moore S, et al. Severe acute respiratory syndrome coronavirus infection causes neuronal death in the absence of encephalitis in mice transgenic for human ACE2. J Virol 2008, 82(15): 7264–7275.
[27]
Seixas AI, Azevedo MM, de Faria JP, et al. Evolvability of the actin cytoskeleton in oligodendrocytes during central nervous system development and aging. Cell Mol Life Sci 2019, 76(1): 1–11.
[28]
Wilson R, Brophy PJ. Role for the oligodendrocyte cytoskeleton in myelination. J Neurosci Res 1989, 22(4): 439–448.
[29]
Kachar B, Behar T, Dubois-Dalcq M. Cell shape and motility of oligodendrocytes cultured without neurons. Cell Tissue Res 1986, 244(1): 27–38.
[30]
Meinhardt J, Radke J, Dittmayer C, et al. Olfactory transmucosal SARS-CoV-2 invasion as a port of central nervous system entry in individuals with COVID-19. Nat Neurosci 2021, 24(2): 168–175.
[31]
Kirtipal N, Bharadwaj S, Kang SG. From SARS to SARS-CoV-2, insights on structure, pathogenicity and immunity aspects of pandemic human coronaviruses. Infect Genet Evol 2020, 85: 104502.
[32]
Jackson CB, Farzan M, Chen B, et al. Mechanisms of SARS-CoV-2 entry into cells. Nat Rev Mol Cell Biol 2022, 23(1): 3–20.
[33]
Wang FZ, Kream RM, Stefano GB. Long-term respiratory and neurological sequelae of COVID-19. Med Sci Monit 2020, 26: e928996.
[34]
Jha NK, Ojha S, Jha SK, et al. Evidence of coronavirus (CoV) pathogenesis and emerging pathogen SARS-CoV-2 in the nervous system: a review on neurological impairments and manifestations. J Mol Neurosci 2021, 71(11): 2192–2209.
[35]
Andalib S, Biller J, Di Napoli M, et al. Peripheral nervous system manifestations associated with COVID-19. Curr Neurol Neurosci Rep 2021, 21(3): 9.
[36]
Karki R, Sharma BR, Tuladhar S, et al. Synergism of TNF-α and IFN-γ triggers inflammatory cell death, tissue damage, and mortality in SARS-CoV-2 infection and cytokine shock syndromes. Cell 2021, 184(1): 149–168.e17.
[37]
Keaney J, Campbell M. The dynamic blood-brain barrier. FEBS J 2015, 282(21): 4067–4079.
[38]
Cheng JP, Korte N, Nortley R, et al. Targeting pericytes for therapeutic approaches to neurological disorders. Acta Neuropathol 2018, 136(4): 507–523.
[39]
Bilinska K, Jakubowska P, Von Bartheld CS, et al. Expression of the SARS-CoV-2 entry proteins, ACE2 and TMPRSS2, in cells of the olfactory epithelium: identification of cell types and trends with age. ACS Chem Neurosci 2020, 11(11): 1555–1562.
[40]
Zubair AS, McAlpine LS, Gardin T, et al. Neuropathogenesis and neurologic manifestations of the coronaviruses in the age of coronavirus disease 2019: a review. JAMA Neurol 2020, 77(8): 1018–1027.
[41]
de F Ferreira ACA, Romão TT, Macedo YS, et al. COVID-19 and Herpes zoster co-infection presenting with trigeminal neuropathy. Eur J Neurol 2020, 27(9): 1748–1750.
[42]
DeOre BJ, Tran KA, Andrews AM, et al. SARS-CoV-2 spike protein disrupts blood-brain barrier integrity via RhoA activation. J Neuroimmune Pharmacol 2021, 16(4): 722–728.
[43]
Thakur KT, Miller EH, Glendinning MD, et al. COVID-19 neuropathology at Columbia university Irving medical center/new york Presbyterian hospital. Brain 2021, 144(9): 2696–2708.
[44]
Mao L, Jin HJ, Wang MD, et al. Neurologic manifestations of hospitalized patients with coronavirus disease 2019 in Wuhan, China. JAMA Neurol 2020, 77(6): 683–690.
[45]
Klok FA, Kruip MA, van der Meer NJM, et al. Incidence of thrombotic complications in critically ill ICU patients with COVID-19. Thromb Res 2020, 191: 145–147.
[46]
Matschke J, Lütgehetmann M, Hagel C, et al. Neuropathology of patients with COVID-19 in Germany: a post-mortem case series. Lancet Neurol 2020, 19(11): 919–929.
[47]
Schurink B, Roos E, Radonic T, et al. Viral presence and immunopathology in patients with lethal COVID-19: a prospective autopsy cohort study. Lancet Microbe 2020, 1(7): e290–e299.
[48]
Moss KR, Bopp TS, Johnson AE, et al. New evidence for secondary axonal degeneration in demyelinating neuropathies. Neurosci Lett 2021, 744: 135595.
[49]
Rahman MA, Islam K, Rahman S, et al. Neurobiochemical cross-talk between COVID-19 and alzheimer’s disease. Mol Neurobiol 2021, 58(3): 1017–1023.
[50]
Cancino GI, Yiu AP, Fatt MP, et al. p63 Regulates adult neural precursor and newly born neuron survival to control hippocampal-dependent Behavior. J Neurosci 2013, 33(31): 12569–12585.
[51]
Abbott NJ, Patabendige AAK, Dolman DEM, et al. Structure and function of the blood-brain barrier. Neurobiol Dis 2010, 37(1): 13–25.
[52]
Hawkins BT, Davis TP. The blood-brain barrier/neurovascular unit in health and disease. Pharmacol Rev 2005, 57(2): 173–185.
[53]
Buzhdygan TP, DeOre BJ, Baldwin-Leclair A, et al. The SARS-CoV-2 spike protein alters barrier function in 2D static and 3D microfluidic in-vitro models of the human blood-brain barrier. Neurobiol Dis 2020, 146: 105131.
[54]
Kimura K, Eguchi S. Angiotensin II type-1 receptor regulates RhoA and Rho-kinase/ROCK activation via multiple mechanisms. Focus on Angiotensin II induces RhoA activation through SHP2-dependent dephosphorylation of the RhoGAP p190A in vascular smooth muscle cells. Am J Physiol Cell Physiol 2009, 297(5): C1059–C1061.
[55]
Bradke F, Roll-Mecak A. Editorial overview: Microtubules in nervous system development. Develop Neurobiol 2021, 81(3): 229–230.
Brain Science Advances
Pages 43-52
Cite this article:
Zhang Q, Jiu Y. The regulation of host cytoskeleton during SARS-CoV-2 infection in the nervous system. Brain Science Advances, 2023, 9(1): 43-52. https://doi.org/10.26599/BSA.2023.9050004

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Received: 17 November 2022
Revised: 30 November 2022
Accepted: 05 December 2022
Published: 27 February 2023
© The authors 2023.

This article is published with open access at journals.sagepub.com/home/BSA

Creative Commons Non Commercial CC BY-NC: This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (http://www.creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage).

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