REPLICATION OF ROTAVIRUS RNA

约翰·T·巴顿是加州大学伯克利分校 微生物学和免疫学以及迈阿密大学医学院。 巴顿博士启动了轮状病毒复制的研究，作为 1984年在南佛罗里达大学担任助理教授，并移居到 他在1987年担任目前的职务。他的研究已经得出了几个 有关轮状病毒RNA复制的出版物。1985年，他收到了一份 美国国立卫生研究院颁发三年R22奖以进行轮状病毒研究 复制。这笔赠款于1989年以竞争性方式续期5年。 好几年了。该部门最近获得了美国国立卫生研究院的培训补助金 申请人为合作者的研究生和博士后。 申请者的直接目标是进一步发展他的研究项目 旨在了解与复制有关的过程 轮状病毒的基因组。他的长期目标是留在学术界 把他的研究努力集中在一项研究的发展上 对阐明事件有重大积极影响的实验室 相对较重的教学和委员会职责让他 有机会将更多的精力集中在追求他的研究目标上。这个 奖励还将提供建立研究所需的时间 与其他大学的研究人员合作，并朝着 培养研究生和博士后。他的求职申请 RCDA得到了他的主席J.Wayne Streilein博士的支持，他 同意减少巴顿博士的部门义务，如果 获奖名单已经公布。 轮状病毒是分段的双链RNA(DsRNA)病毒，是 被认为是多种急性胃肠炎的病原体 包括人类在内的动物。尽管它们对致病很重要，但基本的 轮状病毒的分子生物学还不是很清楚。在以前的 巴顿博士开发了一种支持猿猴的无细胞系统 轮状病毒SA11的RNA复制和转录。病毒的合成 该系统中的dsRNA是不对称的，病毒mRNAs作为 用于负链合成的模板。系统已允许 合成dsRNA的亚病毒颗粒的鉴定和描述 (复制酶粒子)。数据表明，复制酶颗粒是 在大小、密度和蛋白质组成方面是不同的。 复制酶颗粒似乎共享结构蛋白VP1 和VP3以及非结构蛋白NS35、NS34和NS26。一些复制酶 颗粒，除了常见的蛋白质外，还含有VP2，而 其他病毒则含有VP2和VP6。这种异质性显然是由于 当复制酶颗粒合成dsRNA时，它们同时 通过连续的方法将形态塑造成单壳粒子 先加VP2，然后加VP6到含有结构的颗粒中 蛋白质VP1和VP3。巴顿博士提出的研究重点是 为了更全面地描述轮状病毒复制酶的结构 颗粒，与复制酶颗粒相关的蛋白质的功能， 以及病毒mRNA的识别信号，允许它们通过 复制酶颗粒。

John T. Patton is a non-tenured Assistant Professor in the Department of Microbiology and Immunology and the University of Miami School of Medicine. Dr. Patton initiated studies on the replication of the rotaviruses as an Assistant Professor at the University of South Florida in 1984 and moved to his present position in 1987. HIs research has resulted in several publications concerning rotavirus RNA replication. In 1985, he received a three-year R22 award from the NIH to pursue studies on rotavirus replication. The grant was competitively renewed in 1989 for a period of 5 years. The Department was recently awarded an NIH training grant for graduate students and post-doctorates of which the applicant is a co-P.I. The applicant's immediate goal are to further develop his research program aimed at understanding processes involved with the replication of the genome of the rotaviruses. His long term goals are to remain in academia concentrating his research efforts on the development of a research laboratory that has a significant positive impact on elucidating events in the relatively heavy teaching and committee responsibilities allowing him the opportunity to focus more energy into pursuing his research goals. The award would also provide the time required to establish research collaborations with investigators at other universities and towards the training of graduate students and post-doctorates. His application for an RCDA has the support of his chairman, Dr. J. Wayne Streilein, who has agreed to reduce Dr. Patton's departmental obligations in the event that an award is made. Rotaviruses are segmented, double-stranded RNA (dsRNA) viruses that are recognized as causative agents of acute gastroenteritis in a wide variety of animals including man. Despite their pathogenic importance, the basic molecular biology of the rotaviruses is not well understood. In previous work, Dr. Patton developed a cell-free system which supports simian rotavirus SA11 RNA replication and transcription. The synthesis of viral dsRNA in this system is asymmetrical with viral mRNA serving as the template for minus-strand synthesis. The system has allowed the identification and description of subviral particles that synthesize dsRNA (replicase particles). The data indicate that replicase particles are heterogenous with respect to size, density and protein composition. Replicase particles appear to share in common the structural proteins VP1 and VP3 and the nonstructural proteins NS35, NS34 and NS26. Some replicase particles, in addition to the common proteins, also contain VP2 while others contain VP2 and VP6. This heterogeneity apparently arises from the fact that as replicase particles synthesize dsRNA, they concurrently undergo morphogenesis into single-shelled particles by the sequential addition of first VP2 and then VP6 to particles that contain the structural proteins VP1 and VP3. The focus of the research proposed by Dr. Patton is to characterize more completely the structure of rotavirus replicase particles, the function of proteins associated with replicase particles, and the recognition signals of viral mRNA that allow their replication by replicase particles.