Document Type

Article

Publication Date

7-1-2010

Abstract

LDL mediates transfection with plasmid DNA in a variety of cell types in vitro and in several tissues in vivo in the rat. The transfection capacity of LDL is based on apo B100, as arginine/lysine clusters, suggestive of nucleic acid-binding domains and nuclear localization signal sequences, are present throughout the molecule. Apo E may also contribute to this capacity because of its similarity to the Dengue virus capsid proteins and its ability to bind DNA. Synthetic peptides representing two apo B100 regions with prominent Arg/Lys clusters were shown to bind DNA. Region 1 (0014Lys-Ser 0160) shares sequence motifs present in DNA binding domains of Interferon Regulatory Factors and Flaviviridae capsid/core proteins. It also contains a close analog of the B/E receptor ligand of apo E. Region 1 peptides, B1-1 (0014Lys-Glu0054) and B1-2 (0055Leu- Ala0096), mediate transfection of HeLa cells but are cytotoxic. Region 2 (3313Asp-Thr3431), containing the known B/E receptor ligand, shares analog motifs with the human herpesvirus 5 immediate-early transcriptional regulator ( UL122) and Flaviviridae NS3 helicases. Region 2 peptides, B2-1 (3313Asp-Glu3355), and B2-2 (3356Gly-Thr3431) are ineffective in cell transfection and are noncytotoxic.jlr These results confirm the role of LDL as a natural transfection vector in vivo, a capacity imparted by the apo B100, and suggest a basis for Flaviviridae cell entry. Copyright © 2010 by the American Society for Biochemistry and Molecular Biology, Inc.

Comments

This research was originally published in the Journal of Lipid Research. Juan Guevara Jr., Nagindra Prashad, Boris Ermolinsky, John W. Gaubatz, Dongcheul Kang, Andrea E. Schwarzbach, David S. Loose, and Natalia Valentinova Guevara. Apo B100 similarities to viral proteins suggest basis for LDL-DNA binding and transfection capacity. J. Lipid Res. 2010; 51:1704-1718. © the American Society for Biochemistry and Molecular Biology or © the Author(s).

First Page

1704

Last Page

1718

Publication Title

Journal of Lipid Research

DOI

10.1194/jlr.M003277

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.