REPLICATION OF ROTAVIRUS RNA

John T.巴顿是一个非终身助理教授在系 微生物学和免疫学以及迈阿密大学医学院。 博士巴顿发起了轮状病毒复制的研究， 1984年在南佛罗里达大学任助理教授，并搬到 1987年担任现职。 他的研究导致了几个 关于轮状病毒RNA复制的出版物。 1985年，他获得了 美国国立卫生研究院颁发的为期三年的R22奖，用于轮状病毒的研究 复制的 1989年，通过竞争性方式延长了赠款期限， 年 该部门最近获得了NIH培训补助金， 研究生和博士后，其中申请人是一个共同的P.I. 申请人的近期目标是进一步发展他的研究计划 旨在了解涉及复制的过程， 轮状病毒的基因组 他的长期目标是留在学术界 把他的研究精力集中在一项研究的发展上 实验室，对阐明事件有重大积极影响， 相对较重的教学和委员会的责任，使他 有机会集中更多的精力追求他的研究目标。 的 该合同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， 培养研究生和博士后。 他的申请 RCDA得到了他的主席J.韦恩斯特雷林博士的支持， 同意减少巴顿医生的部门义务， 奖已颁发。 轮状病毒是分节的双链RNA（dsRNA）病毒， 被认为是各种急性胃肠炎的病原体 包括人类在内的动物。尽管它们具有致病的重要性， 轮状病毒的分子生物学还不清楚。 前几 巴顿博士开发了一种无细胞系统， 轮状病毒SA11 RNA复制和转录。 病毒的合成 该系统中的dsRNA与病毒mRNA是不对称的， 负链合成模板。 系统允许 合成dsRNA亚病毒颗粒的鉴定和描述 （复制酶颗粒）。 数据表明，复制酶颗粒 在大小、密度和蛋白质组成方面不均匀。 复制酶颗粒似乎共享共同的结构蛋白VP1 以及VP3和非结构蛋白NS35、NS34和NS26。 一些复制酶 除了常见的蛋白质外，颗粒还含有VP2， 其他的含有VP2和VP6。 这种异质性显然是由 事实上，当复制酶颗粒合成dsRNA时， 经历形态发生成单壳颗粒的顺序 首先添加VP2，然后添加VP6至含有结构 蛋白VP1和VP3。 巴顿博士提出的研究重点是 为了更完整地表征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， 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.