NSP5 (rotavirus)

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

NSP5 (rotavirus)
NSP5 (rotavirus)
Identifiers
Symbol	Rota_NS26
Pfam	PF01525
InterPro	IPR002512
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

NSP5 (nonstructural protein 5) encoded by genome segment 11 of group A rotaviruses. In virus-infected cells NSP5 accumulates in the viroplasms. NSP5 has been shown to be autophosphorylated.^[1] Interaction of NSP5 with NSP2 was also demonstrated.^[2] In rotavirus-infected cells, the non-structural proteins NSP5 and NSP2 localize in complexes called viroplasms, where replication and assembly occur and they can drive the formation of viroplasm-like structures in the absence of other rotaviral proteins and rotavirus replication.^[3]

There is no atomic-resolution structure of NSP5 determined as of June 2019. However, the low resolution three-dimensional structure of the NSP2-NSP5 assembly has been observed by cryo-EM. NSP5 occupies the same site as RNA when binding to NSP2. The EM data from this 2006 study has not been published.^[4]

References

^ Afrikanova I, Miozzo MC, Giambiagi S, Burrone O (September 1996). "Phosphorylation generates different forms of rotavirus NSP5". The Journal of General Virology. 77 ( Pt 9) (9): 2059–65. doi:10.1099/0022-1317-77-9-2059. PMID 8811003.
^ Afrikanova I, Fabbretti E, Miozzo MC, Burrone OR (November 1998). "Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2". The Journal of General Virology. 79 (11): 2679–86. doi:10.1099/0022-1317-79-11-2679. PMID 9820143.
^ Fabbretti E, Afrikanova I, Vascotto F, Burrone OR (February 1999). "Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo". The Journal of General Virology. 80 ( Pt 2) (2): 333–9. doi:10.1099/0022-1317-80-2-333. PMID 10073692.
^ Jiang X, Jayaram H, Kumar M, Ludtke SJ, Estes MK, Prasad BV (November 2006). "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication". Journal of Virology. 80 (21): 10829–35. doi:10.1128/JVI.01347-06. PMC 1641785. PMID 16928740.

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[pmid8811003-1] Afrikanova I, Miozzo MC, Giambiagi S, Burrone O (September 1996). "Phosphorylation generates different forms of rotavirus NSP5". The Journal of General Virology. 77 ( Pt 9) (9): 2059–65. doi:10.1099/0022-1317-77-9-2059. PMID 8811003.

[pmid9820143-2] Afrikanova I, Fabbretti E, Miozzo MC, Burrone OR (November 1998). "Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2". The Journal of General Virology. 79 (11): 2679–86. doi:10.1099/0022-1317-79-11-2679. PMID 9820143.

[pmid10073692-3] Fabbretti E, Afrikanova I, Vascotto F, Burrone OR (February 1999). "Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo". The Journal of General Virology. 80 ( Pt 2) (2): 333–9. doi:10.1099/0022-1317-80-2-333. PMID 10073692.

[4] Jiang X, Jayaram H, Kumar M, Ludtke SJ, Estes MK, Prasad BV (November 2006). "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication". Journal of Virology. 80 (21): 10829–35. doi:10.1128/JVI.01347-06. PMC 1641785. PMID 16928740.

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