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鉴定与单纯疱疹病毒 1 包膜蛋白 pUL37 相互作用的宿主细胞蛋白。

Identification of host cell proteins which interact with herpes simplex virus type 1 tegument protein pUL37.

机构信息

Centre for Virus Research, The Westmead Millennium Institute, The University of Sydney, Westmead, NSW, Australia.

出版信息

Biochem Biophys Res Commun. 2012 Jan 20;417(3):961-5. doi: 10.1016/j.bbrc.2011.12.044. Epub 2011 Dec 19.

Abstract

The herpes simplex virus type 1 (HSV-1) structural tegument protein pUL37, which is conserved across the Herpesviridae family, is known to be essential for secondary envelopment during the egress of viral particles. To shed light on additional roles of pUL37 during viral replication a yeast two-hybrid screen of a human brain cDNA library was undertaken. This screen identified ten host cell proteins as potential pUL37 interactors. One of the interactors, serine threonine kinase TAOK3, was subsequently confirmed to interact with pUL37 using an in vitro pulldown assay. Such host cell/pUL37 interactions provide further insights into the multifunctional role of this herpesviral tegument protein.

摘要

单纯疱疹病毒 1 型 (HSV-1) 结构被膜蛋白 pUL37 在疱疹病毒科家族中高度保守,已知其对于病毒颗粒出芽过程中的二次包膜形成至关重要。为了深入了解 pUL37 在病毒复制过程中的其他作用,我们进行了人类大脑 cDNA 文库的酵母双杂交筛选。该筛选鉴定了十个宿主细胞蛋白作为潜在的 pUL37 相互作用蛋白。其中一个相互作用蛋白丝氨酸苏氨酸激酶 TAOK3,随后通过体外下拉实验被确认为与 pUL37 相互作用。这种宿主细胞/pUL37 相互作用进一步深入了解了这种疱疹病毒被膜蛋白的多功能作用。

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