Interactions of heterologous DNA with polyomavirus major structural protein, VP1

FEBS Letters

Forstová, Jitka¹  Štokrová, Jitka²  Griffin, Beverly E.³  Palková, Zdena¹  Korb, Jan²  Fischer, Lukáš¹  Richterová, Zuzana¹ 

[1] Charles University, Faculty of Natural Sciences, Viničná 5, 128 44 Prague 2, Czech Republic;Institute of Molecular Genetics, Czech Academy of Sciences, Flemingovo n.2, 16637 Prague 6, Czech Republic;Imperial College School of Medicine, Hammersmith Hospital, Du Cane Road, London W12 ONN, United Kingdom

关键词: Capsid-like particle;    DNA-protein interaction;    DNA encapsidation;    Gene therapy;    Polyoma virus;    VP1;    major capsid protein;    VP2;    3;    minor capsid proteins;    EM;    electron microscopy;    BAC;    benzyldimethylalkylammonium chloride;   

DOI  :  10.1016/S0014-5793(99)00003-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

‘Empty' polyomavirus pseudocapsids, self-assembled from the major structural protein VP1, bind DNA non-specifically and can deliver it into the nuclei of mammalian cells for expression [Forstová et al. (1995) Hum. Gene Ther. 6, 297–306]. Formation of suitable VP1-DNA complexes appears to be the limiting step in this route of gene delivery. Here, the character of VP1-DNA interactions has been studied in detail. Electron microscopy revealed that VP1 pseudocapsids can create in vitro at least two types of interactions with double-stranded DNA: (i) highly stable complexes, requiring free DNA ends, where the DNA is partially encapsidated; and, (ii) weaker interactions of pseudocapsids with internal parts of the DNA chain.

【 授权许可】

Unknown