Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1
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Publication Details
Output type: Journal article
Author list: Ball JM, Schroeder ME, Williams CV, Schroeder F, Parr RD
Publisher: BioMed Central
Publication year: 2013
Journal: Virology Journal (1743-422X)
Volume number: 10
Number of pages: 15
ISSN: 1743-422X
eISSN: 1743-422X
Languages: English-Great Britain (EN-GB)
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Open access status: gold
Full text URL: https://virologyj.biomedcentral.com/counter/pdf/10.1186/1743-422X-10-336
Abstract
Conclusions: These data show that the cav-1 binding domain is within the hydrophobic face of the NSP4 amphipathic helix. The integrity of the helical structure is important for both cav-1 binding and diarrhea induction implying a connection between NSP4 functional and binding activities.
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