Baudin F, Petit I, Weissenhorn W, Ruigrok R W
EMBL Grenoble Outstation, B.P. 156, 38042 Grenoble Cedex 9, France.
Virology. 2001 Mar 1;281(1):102-8. doi: 10.1006/viro.2000.0804.
Spontaneous proteolysis of influenza virus M1 protein during crystallisation has defined an N-terminal domain of amino acids 1--164. Full-length M1, the N-terminal domain, and the C-terminal part of M1 (residues 165--252) were produced in Escherichia coli. In vitro tests showed that only full-length M1 and its N-terminal domain bind to negatively charged liposomes and that only full-length M1 and its C-terminal part bind to RNP. However, only full-length M1 had transcription inhibition activity. Several independent experimental approaches indicate that in vitro transcription inhibition occurs through polymerisation/aggregation of M1 onto RNP, or of M1 onto M1 already bound to RNP, rather than by binding to a specific active site on the nucleoprotein or the polymerase. The structure/function of influenza virus M1 will be compared with that of the Ebola virus matrix protein, VP40.
流感病毒M1蛋白在结晶过程中的自发蛋白水解作用确定了其1 - 164位氨基酸的N端结构域。全长M1、N端结构域以及M1的C端部分（165 - 252位残基）在大肠杆菌中产生。体外试验表明，只有全长M1及其N端结构域能与带负电荷的脂质体结合，只有全长M1及其C端部分能与核糖核蛋白（RNP）结合。然而，只有全长M1具有转录抑制活性。几种独立的实验方法表明，体外转录抑制是通过M1聚合/聚集到RNP上，或者M1聚合/聚集到已经与RNP结合的M1上，而不是通过与核蛋白或聚合酶上的特定活性位点结合来实现的。将流感病毒M1的结构/功能与埃博拉病毒基质蛋白VP40的结构/功能进行比较。
