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Related Experiment Videos

Herpes simplex virus binds to human serum lipoprotein.

H P Huemer1, H J Menzel, D Potratz

  • 1Department of Hygiene, University of Innsbruck, Austria.

Intervirology
|January 1, 1988
PubMed
Summary

Herpes simplex virus (HSV) type 1 binds to all human serum lipoprotein subclasses. This interaction primarily involves HSV glycoprotein B and the lipid component of lipoproteins.

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Area of Science:

  • Virology
  • Biochemistry
  • Lipid Metabolism

Background:

  • Herpes simplex virus (HSV) is a common human pathogen.
  • Lipoproteins are essential for lipid transport in the blood.
  • The interaction between viruses and host lipoproteins is not fully understood.

Purpose of the Study:

  • To investigate the binding of HSV type 1 to different human serum lipoprotein subclasses.
  • To identify the specific viral and lipoprotein components involved in this interaction.

Main Methods:

  • Purification of human serum lipoproteins using differential ultracentrifugation.
  • Use of artificial proteoliposomes with specific apolipoproteins (A1, E).
  • Enzyme-linked immunosorbent assay (ELISA), column chromatography, and electron microscopy were employed.

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Main Results:

  • HSV type 1 demonstrated significant binding to all tested lipoprotein subclasses (VLDL, LDL, HDL, HDL1).
  • HSV also bound to synthetic proteoliposomes, indicating broad lipid interaction.
  • HSV glycoprotein B was identified as a key viral component binding to lipoproteins.

Conclusions:

  • HSV type 1 readily binds to various human serum lipoproteins.
  • Lipoprotein lipid components and HSV glycoprotein B are the primary interaction partners in HSV-lipoprotein complex formation.