NDLI: A temperature-dependent inhibitory activity of serum on the capacity of Saccharomyces cerevisiae-derived hepatitis B surface antigen to bind to monocytes

Content Provider	Springer Nature Link
Author	Vanlandschoot, P. Van Houtte, F. Roobrouck, A. Stelter, F. Gavilanes, F. Leroux Roels, G.
Copyright Year	2004
Abstract	Hepatitis B surface antigen, when produced in yeast (rHBsAg), is capable of binding to cells that express the lipopolysaccharide coreceptor CD14. This interaction is enhanced by a serum protein, the lipopolysaccharide binding protein (LBP). Here we report that most of the rHBsAg particles that attached to monocytes at 0 °C, were not endocytosed but were released back into the serum-containing binding buffer at 37 °C. Additionally, serum-dependent binding at 37 °C was weak when compared to the serum-dependent attachment at 0 °C. Pre-incubation at 37 °C of cells together with serum did not abolish binding of freshly added rHBsAg at 0 °C. However, pre-incubation of rHBsAg with serum at 37 °C reduced attachment to cells following incubation at 0 °C. Soluble CD14 and LBP, two serum proteins which can act as phospholipid transfer molecules, were shown not to be responsible for the inhibitory effect. Pre-incubation at 37 °C of rHBsAg in serum-free hepatoma cell line-conditioned media resulted in a pronounced reduction in subsequent binding to cells at 0 °C. These observations suggest that the temperature-dependent inhibitory effect is caused by serum factors that are probably secreted by hepatocytes.
Starting Page	247
Ending Page	259
Page Count	13
File Format	PDF
ISSN	03048608
Journal	Archives of Virology
Volume Number	150
Issue Number	2
e-ISSN	14328798
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-10-11
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Medical Microbiology Virology Infectious Diseases
Content Type	Text
Resource Type	Article
Subject	Virology Medicine

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