Gaudier M, Gaudin Y, Knossow M
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif sur Yvette Cedex, France.
Virology. 2001 Sep 30;288(2):308-14. doi: 10.1006/viro.2001.1062.
The matrix protein (M) of vesicular stomatitis virus is responsible for the budding of newly formed virions out of host cells. In vitro, it has been shown to self-associate, a property that may be related to the role of M in virus assembly but also prevents crystallization. Using limited proteolysis by thermolysin, we have isolated and characterized two soluble fragments of the protein that remain noncovalently associated. The digestion product does not self-associate nor is it recruited in aggregates formed by intact M molecules. These results identify a peptide, located at the surface of the protein and disorganized by thermolysin cleavage, responsible for M self-association. The thermolysin-resistant core of M has been crystallized and the crystals diffract to 2-A resolution.
水泡性口炎病毒的基质蛋白（M）负责新形成的病毒粒子从宿主细胞中出芽。在体外，已证明它能自我缔合，这一特性可能与M在病毒组装中的作用有关，但也会阻止结晶。通过嗜热菌蛋白酶进行有限的蛋白水解，我们分离并鉴定了该蛋白的两个保持非共价结合的可溶性片段。消化产物不会自我缔合，也不会被完整的M分子形成的聚集体募集。这些结果确定了位于该蛋白表面且因嗜热菌蛋白酶切割而无序的一个肽，它负责M的自我缔合。M的嗜热菌蛋白酶抗性核心已被结晶，晶体衍射分辨率达到2埃。
