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

A temperature-dependent inhibitory activity of serum on the capacity of Saccharomyces cerevisiae... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

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

Loading next page...
 
/lp/springer_journal/a-temperature-dependent-inhibitory-activity-of-serum-on-the-capacity-PQ8dlOS4pc
Publisher
Springer-Verlag
Copyright
Copyright © 2005 by Springer-Verlag/Wien
Subject
Biomedicine; Medical Microbiology; Virology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-004-0416-6
Publisher site
See Article on Publisher Site

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.

Journal

Archives of VirologySpringer Journals

Published: Feb 1, 2005

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve Freelancer

DeepDyve Pro

Price
FREE
$49/month

$360/year
Save searches from
Google Scholar,
PubMed
Create lists to
organize your research
Export lists, citations
Read DeepDyve articles
Abstract access only
Unlimited access to over
18 million full-text articles
Print
20 pages/month
PDF Discount
20% off