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Epitope specificity of monoclonal anti-beta 2-glycoprotein I antibodies derived from patients with the antiphospholipid syndrome.
J Immunol. 1995 Aug 01; 155(3):1629-36.JI

Abstract

beta 2-Glycoprotein I (beta 2GPI) has been identified as a cofactor in the recognition of the phospholipid Ag cardiolipin (CL) by anticardiolipin Ab (aCL) purified from patients with autoimmune diseases. However, there is considerable controversy as to the exact nature of the epitopes to which these Abs are directed. mAb derived from patients with the antiphospholipid syndrome bound to CL only in the presence of beta 2GPI. Synthetic peptides that span the fifth C-terminal domain of beta 2GPI supported the binding of one of the mAbs to CL in a beta 2GPI-free system. These peptides possessed the phospholipid binding sequence Cys281-Lys-Asn-Lys-Glu-Lys-Lys-Cys288. Three of the mAbs bound to beta 2GPI that had been adsorbed on gamma-irradiated microtiter plates. Binding to beta 2GPI was inhibited in a dose-dependent manner by the peptides from the carboxyl-terminal end of beta 2GPI and soluble beta 2GPI, indicating that the mAb bound to peptides and beta 2GPI in free solution. Thus, mAbs derived from patients with the antiphospholipid syndrome have specificity for epitopes on the fifth domain of beta 2GPI. Our results support the idea that beta 2GPI acts as a primary Ag for these Abs.

Authors+Show Affiliations

Department of Immunology, Allergy, and Infectious Disease, University of New South Wales School of Medicine, St. George Hospital, Kogarah, Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7543528

Citation

Wang, M X., et al. "Epitope Specificity of Monoclonal Anti-beta 2-glycoprotein I Antibodies Derived From Patients With the Antiphospholipid Syndrome." Journal of Immunology (Baltimore, Md. : 1950), vol. 155, no. 3, 1995, pp. 1629-36.
Wang MX, Kandiah DA, Ichikawa K, et al. Epitope specificity of monoclonal anti-beta 2-glycoprotein I antibodies derived from patients with the antiphospholipid syndrome. J Immunol. 1995;155(3):1629-36.
Wang, M. X., Kandiah, D. A., Ichikawa, K., Khamashta, M., Hughes, G., Koike, T., Roubey, R., & Krilis, S. A. (1995). Epitope specificity of monoclonal anti-beta 2-glycoprotein I antibodies derived from patients with the antiphospholipid syndrome. Journal of Immunology (Baltimore, Md. : 1950), 155(3), 1629-36.
Wang MX, et al. Epitope Specificity of Monoclonal Anti-beta 2-glycoprotein I Antibodies Derived From Patients With the Antiphospholipid Syndrome. J Immunol. 1995 Aug 1;155(3):1629-36. PubMed PMID: 7543528.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Epitope specificity of monoclonal anti-beta 2-glycoprotein I antibodies derived from patients with the antiphospholipid syndrome. AU - Wang,M X, AU - Kandiah,D A, AU - Ichikawa,K, AU - Khamashta,M, AU - Hughes,G, AU - Koike,T, AU - Roubey,R, AU - Krilis,S A, PY - 1995/8/1/pubmed PY - 1995/8/1/medline PY - 1995/8/1/entrez SP - 1629 EP - 36 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J Immunol VL - 155 IS - 3 N2 - beta 2-Glycoprotein I (beta 2GPI) has been identified as a cofactor in the recognition of the phospholipid Ag cardiolipin (CL) by anticardiolipin Ab (aCL) purified from patients with autoimmune diseases. However, there is considerable controversy as to the exact nature of the epitopes to which these Abs are directed. mAb derived from patients with the antiphospholipid syndrome bound to CL only in the presence of beta 2GPI. Synthetic peptides that span the fifth C-terminal domain of beta 2GPI supported the binding of one of the mAbs to CL in a beta 2GPI-free system. These peptides possessed the phospholipid binding sequence Cys281-Lys-Asn-Lys-Glu-Lys-Lys-Cys288. Three of the mAbs bound to beta 2GPI that had been adsorbed on gamma-irradiated microtiter plates. Binding to beta 2GPI was inhibited in a dose-dependent manner by the peptides from the carboxyl-terminal end of beta 2GPI and soluble beta 2GPI, indicating that the mAb bound to peptides and beta 2GPI in free solution. Thus, mAbs derived from patients with the antiphospholipid syndrome have specificity for epitopes on the fifth domain of beta 2GPI. Our results support the idea that beta 2GPI acts as a primary Ag for these Abs. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/7543528/Epitope_specificity_of_monoclonal_anti_beta_2_glycoprotein_I_antibodies_derived_from_patients_with_the_antiphospholipid_syndrome_ L2 - https://www.jimmunol.org/lookup/pmidlookup?view=long&pmid=7543528 DB - PRIME DP - Unbound Medicine ER -