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A fusogenic segment of glycoprotein H from herpes simplex virus enhances transfection efficiency of cationic liposomes by Ying Tu; Ji-seon Kim is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract ## Background Low cellular uptake and endosomal escape are regarded as major limitations for nonviral gene delivery. In the present study, we use cationic liposomes incorporating fusogenic peptides from glycoprotein H of herpes simplex virus to improve cellular internalization and endosomal release of cationic liposome‐DNA complexes. ## Methods A synthetic analogue of a fusogenic peptide domain in glycoprotein H from herpes simplex virus was evaluated for __in vitro__ gene delivery. The fusogenicity of the peptide was evaluated by a lipid mixing assay in neutral and acidic environments. The influence of the peptide on cellular internalization and subcellular distribution of Lipofectamine‐pGL3 complexes were evaluated by flow cytometry, fluorescence microscopy, and confocal laser scanning microscopy. The effect of the peptide on transfection efficiency of cationic liposomes was also evaluated by luciferase assay in human cell lines. ## Results A pH‐sensitive fusogenicity of the wild‐type peptide was observed. In the lipid mixing assay, the peptide mediated 80% membrane fusion at pH 7.4 at a 0.05 : 1 (peptide : lipid) mole ratio. At pH 4.5, 100% of membrane fusion was obs

Who reads A fusogenic segment of glycoprotein H from herpes simplex virus enhances transfection efficiency of cationic liposomes?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Ying Tu; Ji-seon Kim
Publisher
John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 1099-498X)
Published
2008
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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