Epitopes on β2-GPI recognized by anticardiolipin antibodies

T. Koike; K. Ichikawa; H. Kasahara; T. Atsumi; A. Tsutsumi; E. Matsuura

doi:10.1177/096120339800700204

Epitopes on β₂-GPI recognized by anticardiolipin antibodies

T. Koike, K. Ichikawa, H. Kasahara, T. Atsumi, A. Tsutsumi, E. Matsuura

Neutron Therapy Research Center

Research output: Contribution to journal › Article › peer-review

42 Citations (Scopus)

Abstract

Anticardiolipin antibodies (aCL) found in sera from patients with antiphospholipid syndrome recognize a cryptic epitope that appears on the β₂-glycoprotein I (β₂-GPI) molecule when β₂-GPI interacts with a lipid membrane composed of negatively charged phospholipid or when β₂-GPI is adsorbed on a polyoxygenated polystyrene plate. A homology based model of β₂-GPI was constructed based on the NMR coordinates of sushi domains of human factor H. The conformation was like a cylinder consisting of five domains, its IV and V domains being glued by electrostatic interaction. We used phage-displayed random peptide libraries to search the epitopes of human aCL. Structures similar to consensus sequences selected by a biopanning method was found on domain IV of β₂-GPI.

Original language	English
Pages (from-to)	S14-S17
Journal	Lupus
Volume	7
Issue number	SUPPL. 2
DOIs	https://doi.org/10.1177/096120339800700204
Publication status	Published - 1998

Keywords

Anticardiolipin antibodies
Epitopes
Structure of β-GPI
β-glycoprotein I

ASJC Scopus subject areas

Rheumatology

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10.1177/096120339800700204

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abstract = "Anticardiolipin antibodies (aCL) found in sera from patients with antiphospholipid syndrome recognize a cryptic epitope that appears on the β2-glycoprotein I (β2-GPI) molecule when β2-GPI interacts with a lipid membrane composed of negatively charged phospholipid or when β2-GPI is adsorbed on a polyoxygenated polystyrene plate. A homology based model of β2-GPI was constructed based on the NMR coordinates of sushi domains of human factor H. The conformation was like a cylinder consisting of five domains, its IV and V domains being glued by electrostatic interaction. We used phage-displayed random peptide libraries to search the epitopes of human aCL. Structures similar to consensus sequences selected by a biopanning method was found on domain IV of β2-GPI.",

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AU - Koike, T.

AU - Ichikawa, K.

AU - Kasahara, H.

AU - Atsumi, T.

AU - Tsutsumi, A.

AU - Matsuura, E.

PY - 1998

Y1 - 1998

N2 - Anticardiolipin antibodies (aCL) found in sera from patients with antiphospholipid syndrome recognize a cryptic epitope that appears on the β2-glycoprotein I (β2-GPI) molecule when β2-GPI interacts with a lipid membrane composed of negatively charged phospholipid or when β2-GPI is adsorbed on a polyoxygenated polystyrene plate. A homology based model of β2-GPI was constructed based on the NMR coordinates of sushi domains of human factor H. The conformation was like a cylinder consisting of five domains, its IV and V domains being glued by electrostatic interaction. We used phage-displayed random peptide libraries to search the epitopes of human aCL. Structures similar to consensus sequences selected by a biopanning method was found on domain IV of β2-GPI.

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