NSP4 (rotavirus)
The rotavirus nonstructural protein NSP4 was the first viral enterotoxin discovered. It induces diarrhea and causes Ca2+-dependent transepithelial secretion.[1]
| NSP4 (rotavirus) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Rota_NSP4 | ||||||||
| Pfam | PF01452 | ||||||||
| InterPro | IPR002107 | ||||||||
| CATH | 1g1iA00 | ||||||||
| SCOPe | 1g1i / SUPFAM | ||||||||
| |||||||||
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.[2]
References
- 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. doi:10.1073/pnas.94.8.3960. PMC 20550. PMID 9108087.
- 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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