STUDIES ON EFFECT OF CHYMOTRYPSIN ON REOVIRIONS
STUDIES ON EFFECT OF CHYMOTRYPSIN ON REOVIRIONS
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DOI：
10.1016/0042-6822(72)90527-2
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发表时间：
1972-01-01
期刊：
影响因子：
3.7
通讯作者：
JOKLIK, WK
中科院分区：
文献类型：
--
作者：
JOKLIK, WK
本文研究了胰凝乳蛋白酶对Dearing、Abney和Carter三株呼肠孤病毒化学和生物学特性的影响，在低酶浓度（病毒浓度不低于100 μ g/ml，酶浓度低于100 μ g/ml）下，胰凝乳蛋白酶可将呼肠孤病毒经几个阶段转化为核心。第一阶段包括去除衣壳多肽σ3，并产生保留完全感染性的颗粒，在37°长时间孵育后失去其寡核苷酸，并且不具有转录酶活性。第二阶段涉及通过一系列连续产生的多肽片段去除多肽μ2，所述多肽片段保持与颗粒瞬时缔合。在此阶段开始时，病毒絮凝，浮力密度增加，比感染性减少约5个对数，失去其寡核苷酸补体，并产生转录酶活性。在最后阶段，颗粒失去多肽σ 1。在高酶浓度下（Abney和Dearing菌株超过1000 μg/ml，Carter菌株超过100 μg/ml），形成不同的终产物。这是由缺乏多肽σ3和μ2的12，000道尔顿片段的颗粒组成的，具有比病毒粒子高约0.01 μ g/ml的浮力密度，并且具有完全感染性，完整的寡核苷酸互补，并且没有转录酶活性。这些颗粒在其物理，酶和生物学特性方面与病毒粒子非常相似，但缺乏约三分之一的衣壳蛋白补体。胰凝乳蛋白酶对reovirions的降解受到悬浮介质离子强度的影响。它也受到病毒浓度的强烈影响，这表明粒子间的相互作用可能起作用。
The effect of chymotrypsin on the chemical and biological properties of three strains of reovirus, namely Dearing, Abney, and Carter, was studied.At low enzyme concentrations (less than 100 μg/ml provided that the virus concentration was not below 100 μg/ml) chymotrypsin converted reovirions to cores via several stages. The first stage consisted of the removal of capsid polypeptide σ3 and yielded particles which retained full infectivity, lost their oligonucleotides on prolonged incubation at 37°, and possessed no transcriptase activity. The second stage involved the removal of polypeptide μ2 via a series of sequentially arising polypeptide fragments which remained transiently associated with the particles. At the beginning of this stage virus flocculated, increased in buoyant density, diminished about 5 logs with respect to specific infectivity, lost its oligonucleotide complement, and developed transcriptase activity. During the final stage the particles lost polypeptide σ1.At high enzyme concentrations (more than 1000 μg/ml for strains Abney and Dearing, and more than 100 μg/ml for Carter) a different end product was formed. This consisted of particles which lacked polypeptide σ3 and a 12,000 dalton fragment of μ2, had a buoyant density about 0.01 g/ml higher than that of virions, and possessed full infectivity, the entire oligonucleotide complement, and no transcriptase activity. These particles closely resembled virions in their physical, enzymatic, and biological properties, but lacked about one-third of their capsid protein complement.The degradation of reovirions by chymotrypsin was affected by the ionic strength of the suspending medium. It was also strongly influenced by virus concentration, suggesting that particle-particle interactions may play a role.