scholarly journals The Hepatitis B Surface Antigen Binding Protein: An Immunoglobulin G Constant Region-Like Protein That Interacts With HBV Envelop Proteins and Mediates HBV Entry

2018 ◽  
Vol 8 ◽  
Author(s):  
Yeping Sun ◽  
Shanshan Wang ◽  
Yong Yi ◽  
Jing Zhang ◽  
Zhongping Duan ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Immunoglobulin G ◽  
Binding Protein ◽  
Hepatitis B Surface Antigen ◽  
Antigen Binding ◽  
Constant Region

Stability and Activity of Intravenous Immunoglobulin with Neonatal Dextrose and Total Parenteral Nutrient Solutions

1994 ◽  
Vol 28 (9) ◽  
pp. 1014-1017
Author(s):  
Christine A. Lindsay ◽  
Ken Dang ◽  
James M. Adams ◽  
Ching Nan Ou ◽  
Carol J. Baker
Keyword(s):  
Hepatitis B ◽  
Intravenous Immunoglobulin ◽  
Surface Antigen ◽  
Immunoglobulin G ◽  
Functional Activity ◽  
Hepatitis B Surface Antigen ◽  
Type Iii ◽  
Apparent Decrease ◽  
Total Immunoglobulin

OBJECTIVE: To determine in vitro the compatibility of reconstituted intravenous immunoglobulin (IVIG) (Gammagard, Baxter-Hyland) with five different neonatal and pediatric intravenous solutions in Viaflex polyvinyl chloride bags. DESIGN: In vitro compatibility study. INTERVENTIONS: Samples were taken at time=0, 10, 30, 60, 90, and 120 minutes and at 4, 8, 12, and 24 hours and assayed for total immunoglobulin G content and antibodies to hepatitis B surface antigen. Type III group B Streptococcus (GBS) and opsonic activity for type III GBS were analyzed at time=0, 60, and 120 minutes and 12 and 24 hours. All results were compared with those from pure IVIG. RESULTS: Our results demonstrate that mixing IVIG with intravenous solutions commonly used in the care of premature infants (dextrose 5% in water [D5W], D15W, D5W/NaCl 0.225%, and total parenteral nutrition [TPN]) does not significantly alter total immunoglobulin G concentrations or concentration of antibodies to hepatitis B surface antigen or type III GBS. As well, the in vitro functional activity for type III GBS of the IVIG, when mixed with these solutions for up to 24 hours, remained intact. An apparent decrease in bactericidal killing was seen with the IVIG/central TPN mixture. This apparent decrease was found to be an artifact of the high concentration of glucose (20 percent) in the solution. CONCLUSIONS: We propose that Gammagard may be mixed with these solutions through Y-site connections without loss of antibody content or functional activity of the IVIG.

Fibronectin and asialoglyprotein receptor mediate hepatitis B surface antigen binding to the cell surface

2010 ◽  
Vol 155 (6) ◽  
pp. 881-888 ◽  
Author(s):  
Jing Yang ◽  
Feng Wang ◽  
Linlin Tian ◽  
Jing Su ◽  
Xiangqian Zhu ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Cell Surface ◽  
Surface Antigen ◽  
Hepatitis B Surface Antigen ◽  
Antigen Binding

scholarly journals LPS-binding protein and CD14-dependent attachment of hepatitis B surface antigen to monocytes is determined by the phospholipid moiety of the particles

2002 ◽  
Vol 83 (9) ◽  
pp. 2279-2289 ◽  
Author(s):  
Peter Vanlandschoot ◽  
Freya Van Houtte ◽  
Annelies Roobrouck ◽  
Ali Farhoudi ◽  
Felix Stelter ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Binding Protein ◽  
Hepatitis B Surface Antigen ◽  
Binding Pocket ◽  
Receptor Interaction ◽  
S Protein ◽  
Hbv Vaccine ◽  
B Virus ◽  
Lps Binding

It was observed recently that recombinant yeast-derived hepatitis B surface antigen (rHBsAg) particles, which contain the S protein only, bind almost exclusively to monocytes. It is shown here that binding requires the presence of the LPS receptor CD14. Furthermore, evidence is presented that a domain on CD14 that is identical to or largely overlaps with the LPS-binding pocket is instrumental for the attachment of rHBsAg. Additionally, it is shown that the heat-labile LPS-binding protein (LBP) catalyses the binding of rHBsAg to the cells. Remarkably, natural plasma-derived HBsAg (pHBsAg) does not have this property. pHBsAg devoid of its lipids and reconstituted with phosphatidylserine or phosphatidylglycerol acquires the characteristic of yeast-derived HBsAg. Clearly, the interaction of rHBsAg with the cell membrane is determined by the presence of charged phospholipids that are absent in pHBsAg. Although a lipid–receptor interaction is suggested, antibody-inhibition experiments suggest a possible involvement of the C-terminal region of the S protein in the interaction with monocytes. The possible implications of these observations for hepatitis B virus (HBV) infection and HBV vaccine efficiency are discussed.

IL10 Promotorpolymorphismen beeinflussen die Hepatitis B Surface Antigen und die Hepatitis A spezifische Immunantwort

2015 ◽  
Vol 41 (08) ◽  
Author(s):  
E Reuss ◽  
N Evers ◽  
N Dietrich ◽  
J Vollmar ◽  
PM Schneider ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Hepatitis A ◽  
Hepatitis B Surface Antigen
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