英國研究人員日前報(bào)告說，他們發(fā)現(xiàn)了相關(guān)蛋白質(zhì)在卡波氏肉瘤病毒復(fù)制中的相互作用，這將有助于研發(fā)治療卡波氏肉瘤新藥。
英國利茲大學(xué)研究人員在新一期《歐洲分子生物學(xué)組織期刊》（The EMBO Journal）上報(bào)告說，他們發(fā)現(xiàn),，引發(fā)卡波氏肉瘤的病毒在入侵人體時(shí)會(huì)指導(dǎo)合成一種名為ORF57的蛋白質(zhì)，這種蛋白質(zhì)與一種PYM蛋白質(zhì)相互作用,，使病毒得以復(fù)制,。如果在實(shí)驗(yàn)中阻止這兩種蛋白質(zhì)之間反應(yīng)，病毒就不能進(jìn)行復(fù)制和擴(kuò)散,。
研究人員懷特豪斯說，這是首次發(fā)現(xiàn)相關(guān)蛋白質(zhì)在卡波氏肉瘤病毒復(fù)制中的作用,，有望在此基礎(chǔ)上研發(fā)阻止病毒復(fù)制的新藥,，進(jìn)而有效治療這種癌癥。
卡波氏肉瘤又名多發(fā)性出血性肉瘤,，是一種血管腫瘤導(dǎo)致的癌癥,。它多發(fā)于免疫系統(tǒng)受損人群,，如艾滋病患者等。目前化療等手段對這種癌癥效果不彰,，且常有副作用,。（生 物 谷Bioon.com）
Bioon.com推薦原文出處：
The EMBO Journal doi:10.1038/emboj.2010.77
Kaposi's sarcoma-associated herpesvirus ORF57 protein interacts with PYM to enhance translation of viral intronless mRNAs
James R Boyne1,3,4, Brian R Jackson1,4, Adam Taylor1, Stuart A Macnab1 and Adrian Whitehouse1,2
1 Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK
2 Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK
3 Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK
Kaposi's sarcoma-associated herpesvirus (KSHV) expresses numerous intronless mRNAs that are unable to access splicing-dependent cellular mRNA nuclear export pathways. To circumvent this problem, KSHV encodes the open reading frame 57 (ORF57) protein, which orchestrates the formation of an export-competent virus ribonucleoprotein particle comprising the nuclear export complex hTREX, but not the exon-junction complex (EJC). Interestingly, EJCs stimulate mRNA translation, which raises the intriguing question of how intronless KSHV transcripts are efficiently translated. Herein, we show that ORF57 associates with components of the 48S pre-initiation complex and co-sediments with the 40S ribosomal subunits. Strikingly, we observed a direct interaction between ORF57 and PYM, a cellular protein that enhances translation by recruiting the 48S pre-initiation complex to newly exported mRNAs, through an interaction with the EJC. Moreover, detailed biochemical analysis suggests that ORF57 recruits PYM to intronless KSHV mRNA and PYM then facilitates the association of ORF57 and the cellular translation machinery. We, therefore, propose a model whereby ORF57 interacts directly with PYM to enhance translation of intronless KSHV transcripts.
