Interaction of human plasma fibronectin with viral proteins of human immunodeficiency virus

FEMS Immunol Med Microbiol. 1994 Feb;8(2):127-31. doi: 10.1111/j.1574-695X.1994.tb00434.x.

Abstract

Fibronectin (FN) is present in soluble and matrix forms in various body fluids and tissues, and has been shown to bind to several pathogens, including viruses. The interaction of FN with viral proteins of human immunodeficiency virus (HIV-1) was investigated by immunofluorescence technique using a cell line chronically infected with HIV-1 (H9-V). The results of this study showed that FN binds to HIV-1 infected cells, especially at FN concentration of 5 micrograms/ml. In addition, FN-pentapeptide has shown the ability to bind to HIV-1 infected cells. On the other hand, preincubation with antibodies against FN abolished the binding of FN to HIV-1 infected cells. Finally, FN has shown to bind to HIV-1 glycoproteins, including gp41 and gp120. In contrast, no binding to HIV-1 core proteins, including p15 and p24, was noted. We suggest that FN, in binding HIV-1 particles, may reduce viremia and thus may be involved in the clearance of viral proteins from the cells.

Publication types

  • Comparative Study

MeSH terms

  • Dose-Response Relationship, Drug
  • Enzyme-Linked Immunosorbent Assay
  • Fibronectins / blood
  • Fibronectins / immunology
  • Fibronectins / metabolism*
  • HIV Envelope Protein gp120 / metabolism*
  • HIV Envelope Protein gp41 / metabolism*
  • HIV-1 / metabolism*
  • Humans
  • Oligopeptides / metabolism
  • Peptide Fragments / metabolism

Substances

  • Fibronectins
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • Oligopeptides
  • Peptide Fragments
  • glycyl-arginyl-glycyl-aspartyl-serine