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Related Experiment Videos

Matrix fibronectin increases HIV stability and infectivity.

Giampaolo Greco1, Sampa Pal, Renata Pasqualini

  • 1Division of Pulmonary and Critical Care Medicine, Mount Sinai School of Medicine, New York, NY 10029, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|May 23, 2002
PubMed
Summary

Matrix-associated fibronectin (FN) and its degraded forms enhance HIV-1 infection of CD4(+) T cells. This effect is independent of coreceptor specificity and prolongs viral infectivity, suggesting a role for FN in HIV pathogenesis.

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Area of Science:

  • Virology
  • Immunology
  • Biochemistry

Background:

  • HIV-1 establishes reservoirs in lymphoid tissues.
  • Previous studies indicated superfibronectin (sFN) and FN fragments enhance HIV-1 infection.

Purpose of the Study:

  • To investigate the role of different fibronectin (FN) conformations in HIV-1 infection.
  • To determine if FN fragments generated by proteolysis enhance HIV-1 infectivity.

Main Methods:

  • Primary CD4(+) T cells and reporter cell lines were used.
  • HIV pseudotyped with different envelope glycoproteins (gp120) were employed.
  • Cells were transfected with CD4 and chemokine receptors.

Main Results:

  • Superfibronectin (sFN) enhanced infection by both R5 and X4 HIV-1 strains.

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  • sFN-mediated enhancement requires the CD4 receptor but does not alter gp120 specificity.
  • Proteolysis of FN by chymotrypsin correlated with enhanced HIV infection.
  • HIV bound to matrix FN maintained infectivity longer than HIV in suspension.

    • Conclusions:

    • Polymerized (matrix) or degraded (inflammation-associated) FN, but not dimeric (plasma) FN, enhances HIV-1 infection.
    • Matrix-bound HIV virions exhibit prolonged infectivity.
    • FN conformation and matrix proteins may influence HIV pathogenesis.