Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1
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چکیده
منابع مشابه
Elucidation of the Rotavirus NSP4-Caveolin-1 and -Cholesterol Interactions Using Synthetic Peptides
Rotavirus (RV) NSP4, the first described viral enterotoxin, is a multifunctional glycoprotein that contributes to viral pathogenesis, morphogenesis, and replication. NSP4 binds both termini of caveolin-1 and is isolated from caveolae fractions that are rich in anionic phospholipids and cholesterol. These interactions indicate that cholesterol/caveolin-1 plays a role in NSP4 transport to the cel...
متن کاملThe rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1.
Rotavirus nonstructural protein 4 (NSP4) is known to function as an intracellular receptor at the endoplasmic reticulum (ER) critical to viral morphogenesis and is the first characterized viral enterotoxin. Exogenously added NSP4 induces diarrhea in rodent pups and stimulates secretory chloride currents across intestinal segments as measured in Ussing chambers. Circular dichroism studies furthe...
متن کاملRotavirus enterotoxin NSP4 binds to the extracellular matrix proteins laminin-beta3 and fibronectin.
Rotavirus is the most important cause of viral gastroenteritis and dehydrating diarrhea in young children. Rotavirus nonstructural protein 4 (NSP4) is an enterotoxin that was identified as an important agent in symptomatic rotavirus infection. To identify cellular proteins that interact with NSP4, a two-hybrid technique with Saccharomyces cerevisiae was used. NSP4 cDNA, derived from the human r...
متن کاملRotavirus Enterotoxin NSP4 Binds to the Extracellular Matrix Proteins Laminin- 3 and Fibronectin
Rotavirus Enterotoxin NSP4 Binds to the Extracellular Matrix Proteins Laminin3 and Fibronectin J. A. Boshuizen, J. W. A. Rossen, C. K. Sitaram, F. F. P. Kimenai, Y. Simons-Oosterhuis, C. Laffeber, H. A. Büller, and A. W. C. Einerhand* Laboratory of Pediatrics, Pediatric Gastroenterology & Nutrition, Erasmus MC/Sophia Children’s Hospital, Rotterdam, and Eijkman-Winkler Institute, Department of V...
متن کاملHigher Expression Level and Lower Toxicity of Genetically Spliced Rotavirus NSP4 in Comparison to the Full-Length Protein in E. coli
Background: Rotavirus group A (RVA) is recognized as a major cause of severe gastroenteritis in children and new-born animals. Nonstructural protein 4 (NSP4) is responsible for the enterotoxic activity of these viruses in the villus epithelial cells. Amino acids 114-135 of NSP4 are known to form the diarrhea-inducing region of this viral enterotoxin. Therefore, developing an NSP4 lacking the en...
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ژورنال
عنوان ژورنال: Virology Journal
سال: 2013
ISSN: 1743-422X
DOI: 10.1186/1743-422x-10-336