The putative cell receptors for hepatitis B virus (HBV), annexin V, and apolipoprotein H, bind to lipid components of HBV.
Annexin V and apolipoprotein H, reported to bind hepatitis B surface antigen (HBsAg) and presumed to react specifically with the HBsAg S protein and to play an important role in initiation of infection by hepatitis B virus, did not bind to delipidated HBsAg (dlHBsAg). Binding activity was restored by adding lipids to dlHBsAg. These results are consistent with the established affinity of annexin V and apolipoprotein H for lipids.
Neurath
A R
AR
Lindsley F. Kimball Research Institute of the New York Blood Center, New York 10021.
Strick
N
N
D017304:Annexin A5 / Q000378:metabolism*; D001053:Apolipoproteins / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006514:Hepatitis B Surface Antigens / Q000378:metabolism; D006515:Hepatitis B virus / Q000378:metabolism*; D007700:Kinetics; D050356:Lipid Metabolism; D008077:Lipoproteins, LDL / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism; D011946:Receptors, Antigen / Q000378:metabolism*; D053482:beta 2-Glycoprotein I
D017304:Annexin A5; D001053:Apolipoproteins; D006023:Glycoproteins; D006514:Hepatitis B Surface Antigens; D008077:Lipoproteins, LDL; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D011946:Receptors, Antigen; D053482:beta 2-Glycoprotein I; C030500:hepatitis B surface antigen receptor