Abstract

Endocytosis of cellular surface membrane proteins is a well-characterized, common occurrence. Internalization of cell surface receptors, often with bound ligands, aid in global events, such as cellular metabolism, as well as in specific, directed functions, such as the induction of signal transduction cascades or immune function. Some, but not all, herpesvirus membrane proteins are internalized from the plasma membrane by a process similar to receptor-mediated endocytosis. No known functions, however, have been ascribed to endocytosis of these proteins. In this review, we consider the function of herpesvirus membrane protein endocytosis. We compare and contrast the endocytosis and intracellular trafficking of two pseudorabies virus membrane proteins, the type I glycoprotein, gE, and the type II, tail-anchored membrane protein, Us9, and discuss the possible function of their internalization during the virus life cycle.

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