- NSP1 (rotavirus)
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NSP1, the product of rotavirus gene 5, is an 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]
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 activating PI3K/Akt survival pathway during early stages of rotavirus infection.[9]
References
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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. doi:10.1073/pnas.0408376102. PMC 554789. PMID 15741273. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=554789.
- ^ 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.
- ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1900170.
- ^ Graff JW, Ettayebi K, Hardy ME (January 2009). Sherry, Barbara. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2627925.
- ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2903281.
DNA RNA capsid: matrix protein (M1 protein) · viral envelope (M2 protein)
glycoprotein: Influenza hemagglutinin · NeuraminidaseParainfluenzaParainfluenza hemagglutinin-neuraminidaseRSVRespiratory syncytial virus G proteinRT VSPs: gag · pol (Integrase, Reverse transcriptase, HIV-1 protease) · env (gp120, gp41)
VRAPs: transactivators (Tat, Rev, Vpr) · Nef · Vif · VpuFusion protein Categories:- Amino acid motifs
- Mutation
- Rotaviruses
- Viral nonstructural proteins
- Viral proteins
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