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The demonstration that the envelope glycoproteins G of vesicular stomatitus virus and hemagglutinin of influenza virus synthesized in polarized epithelial cells transfected with the corresponding genes are effectively segregated to the basolateral or apical plasma membrane domains, respectively, implies that the information determining this segregation resides within the structures of the proteins themselves. To localize the sorting information within these proteins, the polarity of secretion of truncated hemagglutinin and G glycoproteins secreted from confluent monolayers of MDCK cells transformed with vectors containing the corresponding truncated cDNAs was examined. It was found that, even though the transformed cells continued to secrete a major endogenous glycoprotein exclusively from the apical surface, the modified viral glycoproteins were secreted in a nonpolarized fashion from both sides of the monolayers. These observations suggest that important information for the sorting of the viral glycoprotein is contained within their membrane anchoring or cytoplasmic segments or that, if sorting signals are luminally located, these signals must be present in a conformation that is not attainable when the polypeptides are not attached to the membrane.

Nonpolarized secretion of truncated forms of the influenza hemagglutinin and the vesicular stomatitus virus G protein from MDCK cells.