Deletions into an NH2-terminal hydrophobic domain result in secretion of rotavirus VP7, a resident endoplasmic reticulum membrane glycoprotein

Secretion of an Endoplasmic Reticulum Glycoprotein tide function. The NH2-terminal hydrophobic domains seem important in the maturation of rotaviruses since the hydrophobic nature is highly conserved in the VP7 glycoproteins of viruses infecting human, simian, and bovine species (20) , and therefore probably serve some role in anchoring this type of protein in the ER. There is no hydrophobic segment present at the COOH-terminus, a distinctive feature of the glycoproteins of plasma membrane maturing viruses. Our systematic generation of mutants affecting each or both of the hydrophobic regions was aimed at identifying the putative membrane anchor domain responsible for the ER location of the rotavirus VP7 glycoprotein.