Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133, Rome, Italy.
Amino Acids. 2010 May;38(5):1541-7. doi: 10.1007/s00726-009-0375-z. Epub 2009 Nov 2.
Protein-protein interactions play an essential role in the regulation of most cellular processes. The process of viral infection is no exception and many viral pathogenic strategies involve targeting and perturbing host-protein interactions. The characterization of the host protein subnetworks disturbed by invading viruses is a major goal of viral research and may contribute to reveal fundamental biological mechanisms and to identify new therapeutic strategies. To assist in this approach, we have developed a database, VirusMINT, which stores in a structured format most of the published interactions between viral and host proteome. Although SH3 are the most ubiquitous and abundant class of protein binding modules, VirusMINT contains only a few interactions mediated by this domain class. To overcome this limitation, we have applied the whole interactome scanning experiment approach to identify interactions between 15 human SH3 domains and viral proline-rich peptides of two oncogenic viruses, human papillomavirus type 16 and human adenovirus A type 12. This approach identifies 114 new potential interactions between the human SH3 domains and proline-rich regions of the two viral proteomes.
蛋白质-蛋白质相互作用在调节大多数细胞过程中起着至关重要的作用。病毒感染过程也不例外，许多病毒致病策略涉及靶向和扰乱宿主蛋白相互作用。表征受入侵病毒干扰的宿主蛋白子网络是病毒研究的主要目标，这可能有助于揭示基本的生物学机制，并确定新的治疗策略。为了辅助这一方法，我们开发了一个数据库 VirusMINT，它以结构化的格式存储了大多数已发表的病毒和宿主蛋白质组之间的相互作用。尽管 SH3 是最普遍和丰富的一类蛋白质结合模块，但 VirusMINT 仅包含少数由该结构域类介导的相互作用。为了克服这一限制，我们应用全相互作用组扫描实验方法来鉴定 15 个人类 SH3 结构域与两种致癌病毒，人乳头瘤病毒 16 型和人腺病毒 A 型 12 的富含脯氨酸的病毒肽之间的相互作用。这种方法鉴定了人类 SH3 结构域与两种病毒蛋白质组中富含脯氨酸的区域之间的 114 个新的潜在相互作用。
