NSP4 (rotavirus): Difference between revisions
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The [[rotavirus]] [[nonstructural protein]] '''NSP4''' (formerly '''NS28'''<ref name="pmid2548854">{{cite journal |vauthors=Bergmann CC, Maass D, Poruchynsky MS, Atkinson PH, Bellamy AR |title=Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum |journal=The EMBO Journal |volume=8 |issue=6 |pages=1695–703 |date=June 1989 |pmid=2548854 |pmc=401011 |doi= |url=}}</ref> or ''' |
The [[rotavirus]] [[nonstructural protein]] '''NSP4''' (formerly '''NS28'''<ref name="pmid2548854">{{cite journal |vauthors=Bergmann CC, Maass D, Poruchynsky MS, Atkinson PH, Bellamy AR |title=Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum |journal=The EMBO Journal |volume=8 |issue=6 |pages=1695–703 |date=June 1989 |pmid=2548854 |pmc=401011 |doi= |url=}}</ref> or '''NS29'''<ref name="pmid6302311">B. B. Mason, D. Y. Graham, M. K. Estes: ''Biochemical mapping of the simian rotavirus SA11 genome.'' In: ''[[Journal of Virology]].'' Band 46, Nummer 2, Mai 1983, S. 413–423, {{DOI|10.1128/JVI.46.2.413-423.1983}}, PMID 6302311, {{PMC|255143}}.</ref>) was the first viral [[enterotoxin]] discovered.<ref name=pmid9108087>{{cite journal | vauthors = Dong Y, Zeng CQ, Ball JM, Estes MK, Morris AP | title = The rotavirus enterotoxin NSP4 mobilizes intracellular calcium in human intestinal cells by stimulating phospholipase C-mediated inositol 1,4,5-trisphosphate production | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 8 | pages = 3960–5 | date = April 1997 | pmid = 9108087 | pmc = 20550 | doi = 10.1073/pnas.94.8.3960 | bibcode = 1997PNAS...94.3960D | doi-access = free }}</ref> It is a [[viroporin]]<ref name="pmid28256607">{{cite journal |vauthors=Pham T, Perry JL, Dosey TL, Delcour AH, Hyser JM |title=The Rotavirus NSP4 Viroporin Domain is a Calcium-conducting Ion Channel |journal=Scientific Reports |volume=7 |issue= |pages=43487 |date=March 2017 |pmid=28256607 |pmc=5335360 |doi=10.1038/srep43487 |url=}}</ref> and induces diarrhea and causes Ca<sup>2+</sup>-dependent transepithelial secretion.<ref name="pmid35557094">{{cite journal |vauthors=Gebert JT, Hyser J |title=Using Forward and Reverse Genetics to Understand Calcium Dysregulation in Enteric Viral Virulence |journal=FASEB Journal |volume=36 Suppl 1 |issue= |pages= |date=May 2022 |pmid=35557094 |doi=10.1096/fasebj.2022.36.S1.R3214 |s2cid=248633853 |url=}}</ref> |
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A [[transmembrane]] [[glycoprotein]], NSP4 is organized into three main domains: a three-helical TM domain in the [[N-terminus]] (also a [[viroporin]] domain), a central [[cytoplasm]]ic coiled-coil domain for [[multimer]]ization, and an C-terminal flexible region. It can also be secreted out of the cell. As of 2019, only structures of the central domain, which is responsible for diarrhea, has been solved. It [[oligomer]]izes into [[Dimer (chemistry)|dimeric]], [[tetrameric]], [[pentameric]], and even higher-order forms.<ref>{{cite journal | vauthors = Hu L, Crawford SE, Hyser JM, Estes MK, Prasad BV | title = Rotavirus non-structural proteins: structure and function | journal = Current Opinion in Virology | volume = 2 | issue = 4 | pages = 380–8 | date = August 2012 | pmid = 22789743 | pmc = 3422752 | doi = 10.1016/j.coviro.2012.06.003 }}</ref> |
A [[transmembrane]] [[glycoprotein]], NSP4 is organized into three main domains: a three-helical TM domain in the [[N-terminus]] (also a [[viroporin]] domain), a central [[cytoplasm]]ic coiled-coil domain for [[multimer]]ization, and an C-terminal flexible region. It can also be secreted out of the cell. As of 2019, only structures of the central domain, which is responsible for diarrhea, has been solved. It [[oligomer]]izes into [[Dimer (chemistry)|dimeric]], [[tetrameric]], [[pentameric]], and even higher-order forms.<ref>{{cite journal | vauthors = Hu L, Crawford SE, Hyser JM, Estes MK, Prasad BV | title = Rotavirus non-structural proteins: structure and function | journal = Current Opinion in Virology | volume = 2 | issue = 4 | pages = 380–8 | date = August 2012 | pmid = 22789743 | pmc = 3422752 | doi = 10.1016/j.coviro.2012.06.003 }}</ref> |
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Revision as of 07:53, 4 August 2022
| NSP4 (rotavirus) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Rota_NSP4 | ||||||||
| Pfam | PF01452 | ||||||||
| InterPro | IPR002107 | ||||||||
| CATH | 1g1iA00 | ||||||||
| SCOP2 | 1g1i / SCOPe / SUPFAM | ||||||||
| |||||||||
The rotavirus nonstructural protein NSP4 (formerly NS28[1] or NS29[2]) was the first viral enterotoxin discovered.[3] It is a viroporin[4] and induces diarrhea and causes Ca2+-dependent transepithelial secretion.[5]
A transmembrane glycoprotein, NSP4 is organized into three main domains: a three-helical TM domain in the N-terminus (also a viroporin domain), a central cytoplasmic coiled-coil domain for multimerization, and an C-terminal flexible region. It can also be secreted out of the cell. As of 2019, only structures of the central domain, which is responsible for diarrhea, has been solved. It oligomerizes into dimeric, tetrameric, pentameric, and even higher-order forms.[6]
References
- ^ Bergmann CC, Maass D, Poruchynsky MS, Atkinson PH, Bellamy AR (June 1989). "Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum". The EMBO Journal. 8 (6): 1695–703. PMC 401011. PMID 2548854.
- ^ B. B. Mason, D. Y. Graham, M. K. Estes: Biochemical mapping of the simian rotavirus SA11 genome. In: Journal of Virology. Band 46, Nummer 2, Mai 1983, S. 413–423, doi:10.1128/JVI.46.2.413-423.1983, PMID 6302311, PMC 255143.
- ^ Dong Y, Zeng CQ, Ball JM, Estes MK, Morris AP (April 1997). "The rotavirus enterotoxin NSP4 mobilizes intracellular calcium in human intestinal cells by stimulating phospholipase C-mediated inositol 1,4,5-trisphosphate production". Proceedings of the National Academy of Sciences of the United States of America. 94 (8): 3960–5. Bibcode:1997PNAS...94.3960D. doi:10.1073/pnas.94.8.3960. PMC 20550. PMID 9108087.
- ^ Pham T, Perry JL, Dosey TL, Delcour AH, Hyser JM (March 2017). "The Rotavirus NSP4 Viroporin Domain is a Calcium-conducting Ion Channel". Scientific Reports. 7: 43487. doi:10.1038/srep43487. PMC 5335360. PMID 28256607.
- ^ Gebert JT, Hyser J (May 2022). "Using Forward and Reverse Genetics to Understand Calcium Dysregulation in Enteric Viral Virulence". FASEB Journal. 36 Suppl 1. doi:10.1096/fasebj.2022.36.S1.R3214. PMID 35557094. S2CID 248633853.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Hu L, Crawford SE, Hyser JM, Estes MK, Prasad BV (August 2012). "Rotavirus non-structural proteins: structure and function". Current Opinion in Virology. 2 (4): 380–8. doi:10.1016/j.coviro.2012.06.003. PMC 3422752. PMID 22789743.
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