棘鱼毒液抗病毒蛋白水解部位的分离及部分特性研究

G. Borkow, D. Marco, M. Ovadia
{"title":"棘鱼毒液抗病毒蛋白水解部位的分离及部分特性研究","authors":"G. Borkow, D. Marco, M. Ovadia","doi":"10.2174/1874196700801010021","DOIUrl":null,"url":null,"abstract":"The venom of the viper Echis carinatus sochureki suppresses the hemolytic activity of Sendai virus on human erythrocytes, when pre-incubated with the virions prior to their binding to cells. A fraction (C1), with an IC50 of 1.25 �g/ml, was isolated from the venom. Fraction C1 possesses strong azocollase, azocaseinase and gelatinase activity. The proteolytic and anti-hemolytic potency of C1 depends on the period and temperature of incubation. Its antiviral activity is inhibited by Sodium-EDTA but not by PMSF. SDS PAGE of Sendai virus incubated with fraction C1 shows disappearance of several of the virion high molecular weight bands. We suggest that inhibition of the hemolytic activity of the virions is probably a result of the cleavage of viral surface proteins, such as the hemagglutinin-neuraminidase glycoprotein found on the virion envelope that mediates the absorption of the virus to cells.","PeriodicalId":22949,"journal":{"name":"The Open Biology Journal","volume":"37 1","pages":"21-26"},"PeriodicalIF":0.0000,"publicationDate":"2008-08-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":"{\"title\":\"Isolation and Partial Characterization of an Antiviral Proteolytic Fraction from the Venom of Echis Carinatus Sochureki\",\"authors\":\"G. Borkow, D. Marco, M. Ovadia\",\"doi\":\"10.2174/1874196700801010021\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The venom of the viper Echis carinatus sochureki suppresses the hemolytic activity of Sendai virus on human erythrocytes, when pre-incubated with the virions prior to their binding to cells. A fraction (C1), with an IC50 of 1.25 �g/ml, was isolated from the venom. Fraction C1 possesses strong azocollase, azocaseinase and gelatinase activity. The proteolytic and anti-hemolytic potency of C1 depends on the period and temperature of incubation. Its antiviral activity is inhibited by Sodium-EDTA but not by PMSF. SDS PAGE of Sendai virus incubated with fraction C1 shows disappearance of several of the virion high molecular weight bands. We suggest that inhibition of the hemolytic activity of the virions is probably a result of the cleavage of viral surface proteins, such as the hemagglutinin-neuraminidase glycoprotein found on the virion envelope that mediates the absorption of the virus to cells.\",\"PeriodicalId\":22949,\"journal\":{\"name\":\"The Open Biology Journal\",\"volume\":\"37 1\",\"pages\":\"21-26\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2008-08-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Open Biology Journal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2174/1874196700801010021\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Open Biology Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1874196700801010021","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 4

摘要

在仙台病毒与细胞结合之前,将仙台病毒与病毒粒子预先孵育,其毒液可抑制仙台病毒对人红细胞的溶血活性。从毒液中分离出IC50为1.25 μ g/ml的组分(C1)。组分C1具有较强的偶氮结酶、偶氮酪蛋白酶和明胶酶活性。C1的蛋白水解和抗溶血能力取决于孵育的时间和温度。其抗病毒活性被钠- edta抑制,而不被PMSF抑制。用C1段孵育仙台病毒的SDS PAGE显示,病毒粒子的多个高分子量条带消失。我们认为,病毒粒子溶血活性的抑制可能是病毒表面蛋白裂解的结果,例如在病毒粒子包膜上发现的介导病毒向细胞吸收的血凝素-神经氨酸酶糖蛋白。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Isolation and Partial Characterization of an Antiviral Proteolytic Fraction from the Venom of Echis Carinatus Sochureki
The venom of the viper Echis carinatus sochureki suppresses the hemolytic activity of Sendai virus on human erythrocytes, when pre-incubated with the virions prior to their binding to cells. A fraction (C1), with an IC50 of 1.25 �g/ml, was isolated from the venom. Fraction C1 possesses strong azocollase, azocaseinase and gelatinase activity. The proteolytic and anti-hemolytic potency of C1 depends on the period and temperature of incubation. Its antiviral activity is inhibited by Sodium-EDTA but not by PMSF. SDS PAGE of Sendai virus incubated with fraction C1 shows disappearance of several of the virion high molecular weight bands. We suggest that inhibition of the hemolytic activity of the virions is probably a result of the cleavage of viral surface proteins, such as the hemagglutinin-neuraminidase glycoprotein found on the virion envelope that mediates the absorption of the virus to cells.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信