PURIFICATION OF FUSION PROTEIN OF SENDAI VIRUS - ANALYSIS OF NH2-TERMINAL SEQUENCE GENERATED DURING PRECURSOR ACTIVATION
PURIFICATION OF FUSION PROTEIN OF SENDAI VIRUS - ANALYSIS OF NH2-TERMINAL SEQUENCE GENERATED DURING PRECURSOR ACTIVATION
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DOI：
10.1073/pnas.75.6.2737
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发表时间：
1978-01-01
影响因子：
11.1
通讯作者：
WATERFIELD, MD
中科院分区：
文献类型：
--
作者：
GETHING, MJ;WHITE, JM;WATERFIELD, MD
用透镜凝集素-琼脂糖凝胶柱亲和层析分离纯化仙台病毒的两种糖蛋白--血凝素-神经氨酸酶和融合蛋白（F）。F由两条二硫键键连接的多肽链组成，F1和F2，分子量分别为51，000和11，000，每一条含有15%重量的碳水化合物。NH 2-末端序列分析表明F2被封闭，疏水序列NH 2-Phe-Phe-Gly-Ala-Val-Ile-Gly-Ile-Ile-Ala-Leu-Gly-Pro-Ala-Thr-位于F1的氨基末端。该序列在6个位置上与流感病毒血凝素的较小糖肽链HA 2的疏水性NH 2-末端序列相同。F1和HA 2均由前体糖蛋白（F0，仙台病毒; HA 0，流感病毒）的蛋白水解裂解形成。由于这些裂解赋予仙台病毒和流感病毒感染性和仙台病毒诱导细胞与细胞融合的能力，F1和HA 2上的疏水性NH 2末端序列可能在病毒和宿主细胞膜的融合中发挥作用。
The 2 glycoproteins of Sendai virus, the hemagglutinin-neuraminidase and the fusion protein (F), were separated and purified by affinity chromatography on a Lens culinaris lectin-Sepharose column. F consisted of 2 disulfide-bonded blycopolypeptide chains, F1 and F2, of MW 51,000 and 11,000 each of which contained 15% carbohydrate by wt. NH2-terminal sequence analysis showed that F2 was blocked and that the hydrophobic sequence NH2-Phe-Phe-Gly-Ala-Val-Ile-Gly-Ile-Ile-Ala-Leu-Gly-Pro-Ala-Thr- was at the amino terminus of F1. This sequence shows identity at 6 positions with the hydrophobic NH2-terminal sequence of the smaller glycopolypeptide chain, HA2, of the hemagglutinin of influenza virus. Both F1 and HA2 are formed by proteolytic cleavage of precursor glycoproteins (F0, Sendai virus; HA0, influenza virus). Since these cleavages confer infectivity upon both Sendai and influenza viruses and the ability to induce cell-to-cell fusion upon Sendai virus, the hydrophobic NH2-terminal sequences on F1 and HA2 may play a role in fusion of viral and host-cell membranes.