J. Biol. Chem., Vol. 267, Issue 4, 2142-2148, Feb, 1992
A single amino acid deletion at the amino terminus of influenza virus hemagglutinin causes malfolding and blocks exocytosis of the molecule in mammalian cells
CC Chao
Department of Biochemistry, Chang Gung Medical College, Taoyuan, Taiwan, Republic of China.
I am investigating the role of protein folding in the transport of
influenza virus hemagglutinin (HA), a membrane-bound protein, along the
exocytotic pathway. From a previous work (Gething, M.-J., McCammon, K., and
Sambrook, J. (1986) Cell 46, 939-950), it has been shown that a subset of
alterations of the COOH-terminal sequences of the HA molecule inhibit
folding and impede its transport to the cell surface. Current studies
establish that the integrity of the NH2-terminal sequences of the HA is
essential for assembly and transport of the molecule. Mutants lacking just
1 or 2 amino acids immediately COOH-terminal to the signal cleavage site
are translocated and core glycosylated, but also incorrectly folded. The
mutant molecules are not terminally glycosylated and are thus confined
inside the cells. A hypothesis will be presented to explain why sequences
at opposite ends of the HA molecule are essential for the assembly of
native structures and why correct folding is necessary for transport along
the exocytotic pathway of mammalian cells.
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