An altered form of apolipoprotein H binds hepatitis B virus surface antigen most efficiently

Virology
H MehdiMark E Peeples

Abstract

Using recombinant (r)HBsAg as a ligand, we previously found a 46-kDa human plasma protein capable of specific binding, and identified this protein as apolipoprotein H (apo H). Apo H is able to bind to rHBsAg containing only the small S protein, in both ligand blot and enzyme immunoassay systems (H. Mehdi, M.J. Kaplan, F.Y. Anlar, X. Yang, R. Bayer, K. Sutherland, and M.E. Peeples, J. Virol. 68, 2415-2424, 1994). Apo H is a plasma glycoprotein, some of which is associated with lipoproteins, particularly chylomicrons and high-density lipoproteins (HDL). During normal lipid trafficking in the bloodstream, chylomicrons and HDL are targeted to the hepatocyte, the primary host cell for HBV, for degradation. In this report the method of apo H presentation was examined. rHBsAg bound to apo H very poorly if the apo H was coated directly on a microtiter well, or if it was presented in a soluble form. Binding was 100-fold more efficient when apo H was presented as a complex with monoclonal antibody (MAb) P2D4. These results suggest that binding to this MAb alters apo H, making it highly reactive with rHBsAg. Apo H binding to rHBsAg is not dependent on divalent cations and is optimal at pH 6.5-8.0. Removal of lipids from rHBsAg resulted in...Continue Reading

Citations

Mar 6, 2010·Journal of Cancer Research and Clinical Oncology·Xue JingPu-Jun Gao
Jan 14, 2012·Journal of Viral Hepatitis·C-S HsuJ-H Kao
Dec 19, 2000·Biochimica Et Biophysica Acta·A T LeeA J Schroit
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Dec 19, 2007·Cellular Microbiology·Corinna M LeistnerDieter Glebe
Sep 13, 2003·World Journal of Gastroenterology : WJG·Pu-Jun GaoHan-Yi Yang
Feb 17, 2000·Journal of Chromatography. B, Biomedical Sciences and Applications·D TleugabulovaY Fleitas
Mar 5, 2003·Trends in Immunology·Peter Vanlandschoot, Geert Leroux-Roels

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