RECONSTITUTION OF MEMBRANE BUDDING WITH UNILAMELLAR VESICLES

被引：4

作者：

Shnyrova, Anna V. ^{[1
]}

Zimmerberg, Joshua ^{[1
]}

机构：

[1] Eunice Kennedy Shriver Natl Inst Child Hlth & Hum, Cellular & Mol Biol Lab, Program Phys Biol, Bethesda, MD USA

来源：

METHODS IN ENZYMOLOGY; LIPOSOMES, PT F | 2009年 / 464卷

关键词：

NEWCASTLE-DISEASE VIRUS; VESICULAR STOMATITIS-VIRUS; MATRIX PROTEIN; CURVATURE; LIPOSOMES; ENVELOPE; CELLS;

D O I：

10.1016/S0076-6879(09)64004-0

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Enveloped virus particles select their lipid-protein components and egress by budding from the host cell membranes. The matrix protein of many enveloped viruses has been proposed as a crucial element for viral budding; however, molecular mechanisms behind membrane remodeling by the matrix protein are yet to be unraveled. Here, we describe a set of in vitro functional reconstitution assays that allow quantitative evaluation of both, membrane binding and creation of membrane curvature by the matrix protein isolated from Newcastle Disease Virus. Individual budding events orchestrated by the matrix protein can be resolved in real time. The assays may be applied for direct reconstitution of the on-membrane action of cellular proteins involved in membrane curvature induction upon binding in vivo.

引用

页码：55 / 75

页数：21

共 31 条

[1] Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope [J].