The rotavirus nonstructural glycoprotein NSP4 mobilizes Ca2+ from the endoplasmic reticulum
نویسندگان
چکیده
منابع مشابه
Rotavirus nonstructural glycoprotein NSP4 is secreted from the apical surfaces of polarized epithelial cells.
NSP4, a nonstructural glycoprotein encoded by rotavirus, is involved in the morphogenesis of virus particles in the endoplasmic reticulum of infected cells. NSP4 is also implicated in the pathophysiology of rotavirus-induced diarrhea by acting as an enterotoxin. To mediate enterotoxic effects in vivo, NSP4 must be secreted or released from rotavirus-infected cells in a soluble form; however, pr...
متن کاملMutations in rotavirus nonstructural glycoprotein NSP4 are associated with altered virus virulence.
Rotaviruses are major pathogens causing life-threatening dehydrating gastroenteritis in children and animals. One of the nonstructural proteins, NSP4 (encoded by gene 10), is a transmembrane, endoplasmic reticulum-specific glycoprotein. Recently, our laboratory has shown that NSP4 causes diarrhea in 6- to 10-day-old mice by functioning as an enterotoxin. To confirm the role of NSP4 in rotavirus...
متن کاملReceptor activity of rotavirus nonstructural glycoprotein NS28.
Rotavirus morphogenesis involves the budding of subviral particles through the rough endoplasmic reticulum (RER) membrane of infected cells. During this process, particles acquire the outer capsid proteins and a transient envelope. Previous immunocytochemical and biochemical studies have suggested that a rotavirus nonstructural glycoprotein, NS28, encoded by genome segment 10, is a transmembran...
متن کاملProcessing of rotavirus glycoprotein VP7: implications for the retention of the protein in the endoplasmic reticulum
Rotaviruses are icosahedral particles that assemble in the lumen of the endoplasmic reticulum (ER). The viral glycoprotein, VP7, is also directed into this compartment and is retained for assembly onto the surface of viral cores. VP7 is therefore a resident ER glycoprotein with a luminal orientation. The VP7 gene possesses two potential in-frame initiation codons, each preceding a hydrophobic d...
متن کاملGlycoprotein Hormone Assembly in the Endoplasmic Reticulum
Glycoprotein hormone heterodimers are stabilized by their unusual structures in which a glycosylated loop of the -subunit straddles a hole in the -subunit. This hole is formed when a cysteine at the end of a -subunit strand known as the “seatbelt” becomes “latched” by a disulfide to a cysteine in the -subunit core. The heterodimer is stabilized in part by the difficulty of threading the glycosy...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1995
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.69.9.5763-5772.1995