NSP1 (rotavirus)

NSP1, the product of rotavirus gene 5, is a nonstructural RNA-binding protein that contains a cysteine-rich region and is a component of early replication intermediates. RNA-folding predictions suggest that this region of the NSP1 mRNA can interact with itself, producing a stem-loop structure similar to that found near the 5'-terminus of the NSP1 mRNA.[1]

NSP1 (rotavirus)
Identifiers
SymbolRota_NS53
PfamPF00981
InterProIPR002148

The carboxyl-half of the rotavirus nonstructural protein NSP1 is not required for virus replication.[2]

NSP1 could play a role in host range restriction.[3]

The cysteine-rich region of NSP1 is not considered essential for genome segment reassortment with heterologous virus.[4]

NSP1 interacts with IRF3 in the infected cell. NSP1 is an antagonist of the IFN-signaling pathway.[5]

Interferon regulatory factor 3 (IRF3) is a key transcription factor involved in the induction of interferon (IFN) in response to viral infection. NSP1 binds to and targets IRF3 for proteasome degradation early post-infection. IRF3 degradation is dependent on the presence of NSP1 and the integrity of the N-terminal zinc-binding domain, coupled with the regulated stability of IRF3 and NSP1 by the proteasome, collectively support the hypothesis that NSP1 is an E3 ubiquitin ligase.[6]

NSP1 could mediates the degradation of IRF3, IRF5, and IRF7 by recognizing a common element of IRF proteins, thereby allowing NSP1 to act as a broad-spectrum antagonist of IRF function.[7]

NSP1 also inhibits activation of NFkappaB[8]

NSP1 inhibits cellular apoptosis by directly interacting p85 subunit of PI3K and thus activating PI3K/Akt survival pathway during early stages of rotavirus infection.[9][10]

References
  1. Hua J, Mansell EA, Patton JT (September 1993). "Comparative analysis of the rotavirus NS53 gene: conservation of basic and cysteine-rich regions in the protein and possible stem-loop structures in the RNA". Virology. 196 (1): 372–8. doi:10.1006/viro.1993.1492. PMID 8395125.
  2. Hua J, Patton JT (February 1994). "The carboxyl-half of the rotavirus nonstructural protein NS53 (NSP1) is not required for virus replication". Virology. 198 (2): 567–76. doi:10.1006/viro.1994.1068. PMID 8291239.
  3. Dunn SJ, Cross TL, Greenberg HB (August 1994). "Comparison of the rotavirus nonstructural protein NSP1 (NS53) from different species by sequence analysis and northern blot hybridization". Virology. 203 (1): 178–83. doi:10.1006/viro.1994.1471. PMID 8030275.
  4. Okada J, Kobayashi N, Taniguchi K, Urasawa S (1999). "Analysis on reassortment of rotavirus NSP1 genes lacking coding region for cysteine-rich zinc finger motif". Archives of Virology. 144 (2): 345–53. doi:10.1007/s007050050508. PMID 10470258. S2CID 13288814.
  5. Barro M, Patton JT (March 2005). "Rotavirus nonstructural protein 1 subverts innate immune response by inducing degradation of IFN regulatory factor 3". Proceedings of the National Academy of Sciences of the United States of America. 102 (11): 4114–9. Bibcode:2005PNAS..102.4114B. doi:10.1073/pnas.0408376102. PMC 554789. PMID 15741273.
  6. Graff JW, Ewen J, Ettayebi K, Hardy ME (February 2007). "Zinc-binding domain of rotavirus NSP1 is required for proteasome-dependent degradation of IRF3 and autoregulatory NSP1 stability". The Journal of General Virology. 88 (Pt 2): 613–20. doi:10.1099/vir.0.82255-0. PMID 17251580.
  7. Barro M, Patton JT (May 2007). "Rotavirus NSP1 Inhibits Expression of Type I Interferon by Antagonizing the Function of Interferon Regulatory Factors IRF3, IRF5, and IRF7". Journal of Virology. 81 (9): 4473–81. doi:10.1128/JVI.02498-06. PMC 1900170. PMID 17301153.
  8. Graff JW, Ettayebi K, Hardy ME (January 2009). Sherry B (ed.). "Rotavirus NSP1 Inhibits NFκB Activation by Inducing Proteasome-Dependent Degradation of β-TrCP: A Novel Mechanism of IFN Antagonism". PLOS Pathogens. 5 (1): e1000280. doi:10.1371/journal.ppat.1000280. PMC 2627925. PMID 19180189.
  9. Bagchi P, Dutta D, Chattopadhyay S (July 2010). "Rotavirus Nonstructural Protein 1 Suppresses Virus-Induced Cellular Apoptosis To Facilitate Viral Growth by Activating the Cell Survival Pathways during Early Stages of Infection". Journal of Virology. 84 (13): 6834–6845. doi:10.1128/JVI.00225-10. PMC 2903281. PMID 20392855.
  10. Bagchi P, Nandi S, Nayak MK (February 2013). "Molecular Mechanism behind Rotavirus NSP1-Mediated PI3 Kinase Activation: Interaction between NSP1 and the p85 Subunit of PI3 Kinase". Journal of Virology. 87 (4): 2358–2362. doi:10.1128/JVI.02479-12. PMC 3571490. PMID 23221569.
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