tailieunhanh - Báo cáo khoa học: Pleiotrophin inhibits HIV infection by binding the cell surface-expressed nucleolin

The growth factor pleiotrophin (PTN) has been reported to bind heparan sulfate and nucleolin, two components of the cell surface implicated in the attachment of HIV-1 particles to cells. Here we show that PTN inhibits HIV-1 infection by its capacity to inhibit HIV-1 particle attachment to the surface of permissive cells. The b-sheet domains of PTN appear to be implicated in this inhibitory effect on the HIV infection, in particular the domain containing amino acids 60–110. PTN binding to the cell surface is mediated by high and low affinity binding sites | iFEBS Journal Pleiotrophin inhibits HIV infection by binding the cell surface-expressed nucleolin Elias A. Said1 Jose Courty2 Josette Svab1 Jean Delbe2 Bernard Krust1 and Ara G. Hovanessian1 1 UPR 2228 CNRS UFR Biomédicale des Saints-Peres Paris France 2 Laboratoire de Recherche sur la Croissance Cellulaire la Reparation et la Regeneration Tissulaires CRRET FRE CNRS 2412 Universite Paris Valde Marne Creteil France Keywords binding HIV pleiotrophin receptor surface nucleolin Correspondence E. A. said UPR 2228 CNRS UFR Biomedicale des Saints-Peres 45 rue des Saint-Peres 75270 Paris Cedex 06 France Fax 33 142862042 Tel 33 142864136 E-mail Received 11 May 2005 revised 30 June 2005 accepted 18 July 2005 doi The growth factor pleiotrophin PTN has been reported to bind heparan sulfate and nucleolin two components of the cell surface implicated in the attachment of HIV-1 particles to cells. Here we show that PTN inhibits HIV-1 infection by its capacity to inhibit HIV-1 particle attachment to the surface of permissive cells. The b-sheet domains of PTN appear to be implicated in this inhibitory effect on the HIV infection in particular the domain containing amino acids 60-110. PTN binding to the cell surface is mediated by high and low affinity binding sites. Other inhibitors of HIV attachment known to bind specifically surface expressed nucleolin such as the pseudopeptide HB-19 and the cytokine midkine prevent the binding of PTN to its low affinity-binding site. Confocal immunofluorescence laser microscopy revealed that the cross-linking of surface-bound PTN with a specific antibody results in the clustering of cell surface-expressed nucleolin and the colocalization of both PTN and nucleolin signals. Following its binding to surface-nucleolin PTN is internalized by a temperature sensitive mechanism a process which is inhibited by HB-19 and is independent of heparan and chondroitin sulfate proteoglycans. Nevertheless .

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