Liu Yalan, Cui Zongqiang, Zhang Zhiping, Wei Hongping, Zhou Yafeng, Wang Mingli, Zhang Xian-En
State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China.
Virology. 2009 May 25;388(1):68-77. doi: 10.1016/j.virol.2009.03.007. Epub 2009 Apr 5.
The tegument protein pp28 of human cytomegalovirus (HCMV) is essential for the assembly of infectious HCMV virions, but how it functions during the process of HCMV tegumentation and envelopment remains unclear. By using live cell fluorescence resonance energy transfer (FRET) microscopy and yeast two-hybrid assays, we found that another HCMV tegument protein, UL94, was a specific binding partner for pp28. The interaction between pp28 and UL94 was imaged in a punctuate, juxtanuclear compartment, previously designated as the virus assembly compartment (AC). Amino acids 22-43 of pp28 were identified as being responsible for its binding with UL94, while no linear binding site could be found within UL94. The interaction between pp28 and UL94 may serve as a link in the sequential processes of HCMV capsidation, tegumentation and envelopment. This study provides a foundation for further studies into how the HCMV tegument proteins act in the assembly of HCMV virions.
人类巨细胞病毒(HCMV)的被膜蛋白pp28对于感染性HCMV病毒粒子的组装至关重要,但它在HCMV被膜化和包膜化过程中如何发挥作用仍不清楚。通过使用活细胞荧光共振能量转移(FRET)显微镜和酵母双杂交试验,我们发现另一种HCMV被膜蛋白UL94是pp28的特异性结合伴侣。pp28与UL94之间的相互作用在一个点状的、近核区室中成像,该区域先前被指定为病毒组装区室(AC)。pp28的第22 - 43位氨基酸被确定为其与UL94结合的原因,而在UL94中未发现线性结合位点。pp28与UL94之间的相互作用可能是HCMV衣壳化、被膜化和包膜化连续过程中的一个环节。本研究为进一步研究HCMV被膜蛋白如何在HCMV病毒粒子组装中发挥作用奠定了基础。