Ivanova V T, Rakutina R O, Kordiukova L V, Manykin A A, Fedorova N V, Ksenofontov A L, Slepushkin A N
Vopr Virusol. 2006 Mar-Apr;51(2):22-6.
The internal influenza virus proteins M1 and RNP free from surface protein impurities were isolated from subviral particles (virions free from HA and NA ectomenes). The spikeless particles had no propensity to aggregate in the solution at pH 5.0 as compared with native viruses. The subviral particles of B/Hong Kong/330/01 influenza virus, which belonged to B/Victoria/2/87-lineage, were obtained by proteolytic treatment with the enzyme bromelain under the same conditions as in cases of influenza B viruses of B/Jamagata/16/88 lineage. A chromatographic analysis of the tryptic hydrolyzates obtained for matrix (M1) proteins of A(H1N1) and A(H3N2) influenza viruses revealed differences that were greatest between the protein M1 molecules isolated from influenza viruses of different subtypes of hemagglutinine. These findings suggest there are variations in the structure of this conservative internal viral protein M1 during evolution.
从亚病毒颗粒(不含血凝素(HA)和神经氨酸酶(NA)包膜的病毒粒子)中分离出不含表面蛋白杂质的流感病毒内部蛋白M1和核糖核蛋白(RNP)。与天然病毒相比,无刺突颗粒在pH 5.0的溶液中没有聚集倾向。B/香港/330/01流感病毒的亚病毒颗粒属于B/维多利亚/2/87谱系,是在与B/雅加达/16/88谱系的乙型流感病毒相同的条件下,用菠萝蛋白酶进行蛋白水解处理获得的。对A(H1N1)和A(H3N)流感病毒基质(M1)蛋白的胰蛋白酶水解产物进行色谱分析,结果显示,从不同血凝素亚型流感病毒中分离出的M1蛋白分子之间的差异最大。这些发现表明,这种保守的病毒内部蛋白M1在进化过程中结构存在差异。