Bunyaviridae nonstructural S proteins

Last updated

Bunyaviridae nonstructural S proteins (NSs) are synthesized by viral DNA/RNA and do not play a role in the replication or the viral protein coating. [1] The nonstructural S segment (NSs) created by Bunyaviridae virus family, are able to interact with the human immune system, in order to increase their replication in infected cells. [2] Understanding this mechanism can have global health impacts. [3]

Contents

Inhibition pathways

Within the Bunyaviridae virus family, specifically phlebovirus genus, there has been multiple pathways of the inhibition of the immune response. [3] NSs proteins are able to interact with interferon (INF) pathways, but the mechanism varies from virus to virus. [4] The NSs protein in different viruses have been shown to differ in amino acid sequence by up to 85%. [5]

Rift Valley Fever Virus (RVFV)

NSs protein is distributed throughout the cytoplasm and nucleus of the RVFV-infected cell. The protein created fiber-like substances within the nucleus. [3] NSs in RVFV to the SAP30 region of DNA in the nucleus of the cell, which is an important promotor region of INF-b. [6] Many other NSs proteins in the Bunyaviridae virus family do not function in this same way. [5]

Severe Fever with Thrombocytopenia Syndrome Virus (SFTSV)

Although the exact target of the SFTSV is unknown, many believe that the virus attacks human hemopoietic cells. [7] It has been shown that upstream molecules of INFs are unchanged in infected cells, such as MAVS, TRAF6 and TRAF3. [7] This suggests that INFs are still being produced, but they have no effect and are undetectable in people's blood serum. [6] The NSs protein in SFTSV has been shown to interfere with TBK1 which is needed in the activation of both IRF and NF-κB pathways. [7]

Uukuniemi virus (UUKV)

UUKV is a non-human pathogen that still creates a NSs protein. [5] The NSs protein has only been shown to weakly interact with the 40s subunit of ribosomes and MAVS. [8] [9] [10]

Arumowot virus (AMTV)

AMTV is another non-human pathogen and its NSs protein is quickly degraded by proteasomes, and therefore doesn't cause infection in humans. [11]

References

  1. ↑ Viral+Nonstructural+Proteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  2. ↑ ZHANG, S.; ZHENG, B.; WANG, T.; LI, A.; WAN, J.; QU, J.; LI, CH.; LI, D.; LIANG, M. (2017). "NSs protein of severe fever with thrombocytopenia syndrome virus suppresses interferon production through different mechanism than Rift Valley fever virus". Acta Virologica. 61 (3): 289–298. doi: 10.4149/av_2017_307 . ISSN   1336-2305. PMID   28854793.
  3. 1 2 3 Wu, Xiaodong; Qi, Xian; Liang, Mifang; Li, Chuan; Cardona, Carol J.; Li, Dexin; Xing, Zheng (2014). "Roles of viroplasm-like structures formed by nonstructural protein NSs in infection with severe fever with thrombocytopenia syndrome virus". The FASEB Journal. 28 (6): 2504–2516. doi: 10.1096/fj.13-243857 . ISSN   1530-6860. PMID   24599967. S2CID   20158858.
  4. ↑ Chaudhary, Vidyanath; Zhang, Shuo; Yuen, Kit-San; Li, Chuan; Lui, Pak-Yin; Fung, Sin-Yee; Wang, Pei-Hui; Chan, Chi-Ping; Li, Dexin; Kok, Kin-Hang; Liang, Mifang (2015). "Suppression of type I and type III IFN signalling by NSs protein of severe fever with thrombocytopenia syndrome virus through inhibition of STAT1 phosphorylation and activation" . Journal of General Virology. 96 (11): 3204–3211. doi:10.1099/jgv.0.000280. hdl: 10722/216602 . ISSN   1465-2099. PMID   26353965.
  5. 1 2 3 Leventhal, Shanna S.; Wilson, Drew; Feldmann, Heinz; Hawman, David W. (February 2021). "A Look into Bunyavirales Genomes: Functions of Non-Structural (NS) Proteins". Viruses. 13 (2): 314. doi: 10.3390/v13020314 . PMC   7922539 . PMID   33670641.
  6. 1 2 May, Nicolas Le; Mansuroglu, Zeyni; Léger, Psylvia; Josse, Thibaut; Blot, Guillaume; Billecocq, Agnès; Flick, Ramon; Jacob, Yves; Bonnefoy, Eliette; Bouloy, Michèle (2008-01-25). "A SAP30 Complex Inhibits IFN-β Expression in Rift Valley Fever Virus Infected Cells". PLOS Pathogens. 4 (1): e13. doi: 10.1371/journal.ppat.0040013 . ISSN   1553-7374. PMC   2323286 . PMID   18225953.
  7. 1 2 3 Qu, Bingqian; Qi, Xian; Wu, Xiaodong; Liang, Mifang; Li, Chuan; Cardona, Carol J.; Xu, Wayne; Tang, Fenyang; Li, Zhifeng; Wu, Bing; Powell, Kira (2012-08-15). "Suppression of the Interferon and NF-κB Responses by Severe Fever with Thrombocytopenia Syndrome Virus". Journal of Virology. 86 (16): 8388–8401. doi:10.1128/JVI.00612-12. PMC   3421730 . PMID   22623799.
  8. ↑ Rezelj, Veronica V.; Överby, Anna K.; Elliott, Richard M. (2015). "Generation of Mutant Uukuniemi Viruses Lacking the Nonstructural Protein NSs by Reverse Genetics Indicates that NSs Is a Weak Interferon Antagonist". Journal of Virology. 89 (9): 4849–4856. doi:10.1128/JVI.03511-14. PMC   4403475 . PMID   25673721.
  9. ↑ Simons, J F; Persson, R; Pettersson, R F (1992-07-01). "Association of the nonstructural protein NSs of Uukuniemi virus with the 40S ribosomal subunit". Journal of Virology. 66 (7): 4233–4241. doi:10.1128/jvi.66.7.4233-4241.1992. PMC   241227 . PMID   1534850.
  10. ↑ Rezelj, Veronica V.; Li, Ping; Chaudhary, Vidyanath; Elliott, Richard M.; Jin, Dong-Yan; Brennan, Benjamin (2017). "Differential Antagonism of Human Innate Immune Responses by Tick-Borne Phlebovirus Nonstructural Proteins". mSphere. 2 (3): e00234–17. doi:10.1128/mSphere.00234-17. PMC   5489658 . PMID   28680969.
  11. ↑ Hallam, Hoai J.; Lokugamage, Nandadeva; Ikegami, Tetsuro (2019-11-21). "Rescue of infectious Arumowot virus from cloned cDNA: Posttranslational degradation of Arumowot virus NSs protein in human cells". PLOS Neglected Tropical Diseases. 13 (11): e0007904. doi: 10.1371/journal.pntd.0007904 . ISSN   1935-2735. PMC   6894884 . PMID   31751340.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.