Recombinant hepatitis B surface antigen and anionic phospholipids share a binding region in the fifth domain of beta 2-glycoprotein I (apolipoprotein H)

Haider Mehdi; Asma Naqvi; M. Ilyas Kamboh

doi:10.1016/j.bbadis.2008.01.001

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Recombinant hepatitis B surface antigen and anionic phospholipids share a binding region in the fifth domain of beta 2-glycoprotein I (apolipoprotein H)

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Recombinant hepatitis B surface antigen and anionic phospholipids share a binding region in the fifth domain of beta 2-glycoprotein I (apolipoprotein H)

Haider Mehdi, Asma Naqvi and M. Ilyas Kamboh

Biochimica et biophysica acta. Molecular basis of disease, Vol.1782(3), pp.163-168

03/01/2008

DOI: 10.1016/j.bbadis.2008.01.001

PMCID: PMC2350185

PMID: 18230366

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Abstract

Human beta(2)-glycoprotein I (beta(2)GPI) binds to recombinant hepatitis B surface antigen (rHBsAg), but the location of the binding domain on beta(2)GPI is unknown. It has been suggested that the lipid rather than the protein moiety of rHBsAg binds to beta(2)GPI. Since beta(2)GPI binds to anionic phospholipids (PL) through its lipid-binding region in the fifth domain of 1 beta(2)GPI, we predicted that this lipid-binding region may also be involved in binding rHBsAg. In this study, we examined rHBsAg binding to two naturally occurring mutants of beta(2)GPI, Cys306GIy and Trp316Ser, or evolutionarily conserved hydrophobic amino acid sequence, Leu313-Ala314-Phe315 in the fifth domain Of beta(2)GPI. The two naturally occurring mutations and two mutagenized amino acids, Leu313GIy or Phe315Ser, disrupted the binding of recombinant beta(2)GPI (r beta(2)GPI) to both rHBsAg and cardiolipin (CL), an anionic PL. These results suggest that rHBsAg and CL share the same region in the fifth domain of beta(2)GPI. Credence to this conclusion was further provided by competitive ELISA, where CL-bound r beta(2)GPI was incubated with increasing amounts of rHBsAg. As expected, pre-incubation of r beta(2)GPI with CL precluded binding to rHBsAg, indicating that CL and rHBsAg bind to the same region on beta(2)GPI. Our data provide evidence that the lipid (PL) rather than the protein moiety of rHBsAg binds to beta(2)GPI and that this binding region is located in the fifth domain of beta(2)GPI, which also binds to anionic PL. (C) 2008 Elsevier B.V. All rights reserved.

Biochemistry & Molecular Biology

Biophysics

Cell Biology

Life Sciences & Biomedicine

Science & Technology

Details

Title: Subtitle: Recombinant hepatitis B surface antigen and anionic phospholipids share a binding region in the fifth domain of beta 2-glycoprotein I (apolipoprotein H)
Creators: Haider Mehdi - University of Pittsburgh
Asma Naqvi - University of Pittsburgh
M. Ilyas Kamboh - University of Pittsburgh
Resource Type: Journal article
Publication Details: Biochimica et biophysica acta. Molecular basis of disease, Vol.1782(3), pp.163-168
DOI: 10.1016/j.bbadis.2008.01.001
PMID: 18230366
PMCID: PMC2350185
NLM abbreviation: Biochim Biophys Acta Mol Basis Dis
ISSN: 0925-4439
eISSN: 1879-260X
Publisher: Elsevier
Number of pages: 6
Grant note: R01HL054900 / NATIONAL HEART, LUNG, AND BLOOD INSTITUTE; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI) HL 54900; R01 HL054900; R01 HL054900-10 / NHLBI NIH HHS; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI)
Language: English
Date published: 03/01/2008
Academic Unit: Cardiovascular Medicine; Internal Medicine
Record Identifier: 9984359917802771

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