The large external domain is sufficient for the correct sorting of secreted or chimeric influenza virus hemagglutinins in polarized monkey kidney cells.

Abstract

MA104.11 rhesus kidney cells express several characteristics of polarized epithelial cells, including the formation of "domes" on impermeable substrates, the establishment of a transmonolayer electrical resistance when grown on collagen gels, the polarized maturation of influenza and vesicular stomatitis viruses, and the expression of the glycoproteins of those viruses at a single surface domain. The polarized expression of the influenza virus hemagglutinin (HA) is maintained in MA104.11 cells infected with SV40-derived vectors carrying a cDNA gene for either the wild-type influenza virus HA, a truncated HA gene encoding a secreted form of HA (HAsec), or a chimeric gene encoding a hybrid protein with the external domain of the HA and the transmembrane and cytoplasmic domains of the vesicular stomatitis virus G protein (HAG). Thus, the recognition event separating glycoproteins, such as HA, destined for the apical surface from proteins, such as G, destined for the basolateral membranes involves features of the external domains of the proteins. The transmembrane and cytoplasmic domains of HA have no role in this process.