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FOR THE RECORD

Heparin binding by the HIV-1 tat protein transduction domain

Department of Biochemistry and Molecular Biology, University of Illinois at Chicago, Chicago, Illinois 60612, USA

Reprint requests to: Michael Caffrey, Department of Biochemistry, University of Illinois at Chicago, 1819 W. Polk St., Chicago, IL 60612; email: caffrey{at}uic.edu; fax: (312) 413-0364.

The protein transduction domain from the HIV-1 tat protein (termed PTD-tat) has been fused to the C-terminus of a model cargo protein, the IgG binding domain of streptococcal protein G. We demonstrate that PG-Ctat (PTD-tat fused to the C-terminus of protein G) binds to a heparin affinity column. PG-Ctat binds with relatively high affinity, as shown by its elution at 1.6 M NaCl. The heparin binding properties of PTD-tat are consistent with the idea that heparan sulfate, an analog of heparin found at the cell surface, plays a role in the translocation of PTD-tat fusions. We suggest that the heparin-binding properties of PTD-tat can be exploited for purification of PTD-tat fusions in the absence of affinity tags.

Keywords: Heparan sulfate; heparin; HIV; protein transduction; tat

Abbreviations: IPTG, isopropyl-b-D-thiogalactopyranoside • PG, IgG binding domain of streptococcal protein G • PG-Ctat, HIV-1 tat PTD domain fused to C-terminus of PG • PTD, protein transduction domain • PTD-tat, HIV-1 tat PTD domain

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