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J Biol Chem, Vol. 273, Issue 40, 25612-25615, October 2, 1998
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From the Several studies have demonstrated protein-protein
interactions between microsomal triglyceride transfer protein (MTP) and apolipoprotein B (apoB). However, the binding sites involved in these
interactions have not been elucidated. To identify an MTP binding site
in apoB, we have expressed several apoB sequences as fusion proteins
with the eight-amino acid FLAG peptide. The chimeras were transiently
expressed in COS cells, and conditioned media were used to study the
binding of these sequences to either immobilized or soluble MTP. A
polypeptide containing amino acids 270-570 (B:270-570), but not
1-300, bound to MTP. AGI-S17, an antagonist of apoB-MTP binding,
inhibited the binding of B:270-570 to MTP but not to M2, a monoclonal
antibody that recognizes the FLAG peptide. These data indicated that
B:270-570 contains an MTP binding site. Next, sequences within
270-570 were subjected to C-terminal truncations at natural proline
residues. B:270-509 bound less efficiently than B:270-570, whereas,
B:270-430 and other shorter chimeras did not bind to MTP. Furthermore,
truncations at amino acids 502 and 509 decreased MTP binding by 73 and
42%, respectively. These data indicate that B:430-570 in the
Departments of Pathology and Biochemistry,
Allegheny University of the Health Sciences, MCP-Hahnemann School
of Medicine, Philadelphia, Pennsylvania 19129 and Department of
Pathology, Wake Forest University School of Medicine,
Winston-Salem, North Carolina 27103
1-globular domain of apoB plays a crucial role in
MTP binding and presumably in the initiation and maturation of
apoB-containing lipoproteins.
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