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Binding of fibronectin to viral proteins of HIV-1.

Pugliese A, Torre D, Marietti G, Ferrario G, Speranza F, Biglino A, Zeroli C; International Conference on AIDS.

Int Conf AIDS. 1992 Jul 19-24; 8: A7 (abstract no. PoA 2029).

Inst. Infect. Dis., Turin, Italy.

OBJECTIVES: Fibronectin is a glycoprotein found as a soluble dimer(FN) in plasma and as an insoluble multimer in intercellular matrix. FN acts as an opsonin by binding to several organisms. We have demonstrated that a significant decrease in FN levels was observed in patients with HIV-1 infection. This study was designed to determine binding of FN and FN-peptide(Gly-Arg-Gly-Asp-Ser) to HIV-1 or to viral proteins. METHODS: Infected H9-V cells were treated with various doses of FN and FN-peptide, then challenged with mAb to gp120 and finally stained with rabbit antimouse IgG fluorescein conjugated Abs. Binding of FN to viral proteins was detected by an Elisa system(HIV-1-pentElisa, Biochrom KG, Berlin, Germany). RESULTS: FN bound to H9-V cells especially at doses of 5 and 50 micrograms/mL (P = .008 and P = .02 respectively). In addition, FN-peptide bound to H9-V cells at doses of 5 and 25 micrograms/mL (P = .02). FN, at doses of 1 and 10 micrograms/mL, was able to binding to gp120 of HIV-1, and in a lesser extent, to gp41. On the contrary, FN did not bind to core proteins of HIV-1 (p15, p18 and p24). DISCUSSION: Our data show that FN and FN-peptide bind to H9-V cells through gp120 expressed on their surface. This finding was confirmed by binding of FN to purified gp120 in an Elisa system. It has been reported that an homologous peptide to FN-peptide was found in a polypeptide chain encoded by HIV. It is conceivable that FN, in binding HIV-1 particles, may reduce viremia and may be involved in the clearance of viral proteins from the cells. The interaction of viral proteins with FN may play a role in the opsonization of HIV-1 in vivo or in virus-cell interactions. Cellular fibronectin (insoluble form) could represents a possible receptor to cells that do not express specific receptors to HIV-1.

Publication Types:
  • Meeting Abstracts
Keywords:
  • Animals
  • Berlin
  • Enzyme-Linked Immunosorbent Assay
  • Extracellular Matrix
  • Fibronectins
  • Germany
  • HIV
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp160
  • HIV Envelope Protein gp41
  • HIV Infections
  • HIV Long Terminal Repeat
  • HIV-1
  • Humans
  • Rabbits
  • genetics
  • immunology
  • metabolism
  • pharmacokinetics
Other ID:
  • 92400713
UI: 102198426

From Meeting Abstracts




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