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鼠肝炎病毒E蛋白的病毒孔蛋白活性

Viroporin activity of murine hepatitis virus E protein.

作者信息

Madan Vanessa, García Meritxell de Jesús, Sanz Miguel A, Carrasco Luis

机构信息

Centro de Biología Molecular (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain.

出版信息

FEBS Lett. 2005 Jul 4;579(17):3607-12. doi: 10.1016/j.febslet.2005.05.046.

Abstract

The viroporin activity of the E protein from murine hepatitis virus (MHV), a member of the coronaviruses, was analyzed. Viroporins are a growing family of viral proteins able to enhance membrane permeability, promoting virus budding. Initially, the MHV E gene was inducibly expressed in Escherichia coli cells, leading to the arrest of bacterial growth, cell lysis and permeabilization to different compounds. Thus, exit of labeled nucleotides from E. coli cells to the cytoplasm was apparent upon expression of MHV E. In addition, enhanced entry of the antibiotic hygromycin B occurred at levels comparable to those observed with the viroporin 6K from Sindbis virus. Mammalian cells are also readily permeabilized by the expression of MHV E protein. Finally, brefeldin A powerfully blocks the viroporin activity of the E protein in BHK cells, suggesting that an intact vesicular system is necessary for this coronavirus to permeabilize mammalian cells.

摘要

对冠状病毒成员之一的鼠肝炎病毒(MHV)的E蛋白的病毒孔蛋白活性进行了分析。病毒孔蛋白是一类不断增加的病毒蛋白家族,能够增强膜通透性,促进病毒出芽。最初,MHV E基因在大肠杆菌细胞中可诱导表达,导致细菌生长停滞、细胞裂解以及对不同化合物的通透性增加。因此,在表达MHV E时,标记的核苷酸从大肠杆菌细胞进入细胞质是明显的。此外,抗生素潮霉素B的进入增强,其水平与在辛德毕斯病毒的病毒孔蛋白6K中观察到的水平相当。哺乳动物细胞也很容易因MHV E蛋白的表达而被通透化。最后,布雷菲德菌素A强烈阻断BHK细胞中E蛋白的病毒孔蛋白活性,这表明完整的囊泡系统对于这种冠状病毒通透化哺乳动物细胞是必要的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4e05/7164024/d776a38ffdd9/FEB2-579-3607-g001.jpg

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