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Human beta2-glycoprotein I as an anticardiolipin cofactor determined using
mutants expressed by a baculovirus system
M Igarashi, E Matsuura, Y Igarashi, H Nagae, K Ichikawa, DA Triplett and T Koike
Microbiology Laboratory, Yamasa Corp, Choshi, Japan.
beta2-Glycoprotein I (beta2-GPI) consists of five repeats of a homologous
domain. We designed a series of human beta2-GPI mutant genes, ie, three
mutant genes lacking the domain(s) present in the NH2- terminal region and
two of those present in the COOH-terminal region. These mutant genes were
expressed in Spodoptera frugiperda insect cells (Sf9) infected with
recombinant baculoviruses and the mutant proteins were secreted into the
culture medium. The molecular mass of the purified mutant proteins,
estimated by sodium dodecyl sulfate- polyacrylamide gel electrophoresis,
was fairly consistent with the size calculated from their nucleotide
sequences. Binding of beta2-GPI to solid-phase cardiolipin (CL) was
diminished by the deletion of the fifth domain (domain V) from its complete
structure. Thus, the phospholipid binding site of beta2-GPI is located on
its domain V. Monoclonal anti-CL antibodies (aCL) derived either from NZW x
BXSB (WB) F1 mice or from patients with antiphospholipid syndrome bound
directly to the domain V-deleted mutant protein (DI-IV) absorbed not only
on an oxygenated but also on a plain polystyrene surface. We conclude from
this study that the epitope for aCL is exposed on a conformationally
changed structure of beta2-GPI by interacting with negatively charged
phospholipid or on the mutant protein, DI-IV.
Volume 87,
Issue 8,
pp. 3262-3270,
04/15/1996
Copyright © 1996 by The American Society of Hematology
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