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The cDNA encoding the NH
Volume 270,
Number 23,
Issue of June 9, pp. 14220-14228, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-terminal 589 amino acids of
the extracellular domain of the human polymeric immunoglobulin receptor
was inserted into transfer vectors to generate recombinant baculo- and
vaccinia viruses. Following infection of insect and mammalian cells,
respectively, the resulting truncated protein corresponding to human
secretory component (hSC) was secreted with high efficiency into
serum-free culture medium. The Sf9 insect cell/baculovirus system
yielded as much as 50 mg of hSC/liter of culture, while the mammalian
cells/vaccinia virus system produced up to 10 mg of protein/liter. The
M
of recombinant hSC varied depending on the cell
line in which it was expressed (70,000 in Sf9 cells and 85-95,000
in CV-1, TK- 143B and HeLa). These variations in M resulted from different glycosylation patterns, as evidenced by
endoglycosidase digestion. Efficient single-step purification of the
recombinant protein was achieved either by concanavalin A affinity
chromatography or by Ni-chelate affinity
chromatography, when a 6xHis tag was engineered to the carboxyl
terminus of hSC. Recombinant hSC retained the capacity to specifically
reassociate with dimeric IgA purified from hybridoma cells.
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