SYNTHESIS PROCESSING AND FUNCTION OF HUMAN RSV PROTEINS

人 RSV 蛋白的合成加工和功能

• 批准号: 3818272
• 负责人: P L COLLINS
• 金额: --
• 依托单位: NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3818272
• 关键词: Pneumovirus; carbohydrate transport; gene expression; genetic manipulation; genetic mapping; glycosylation; immunogenetics; membrane activity; membrane proteins; mutagens; protein biosynthesis; protein sequence; thrombospondins; virus antigen; virus genetics; virus protein

The structure and processing of the small 1A protein of human respiratory syncytial virus (RSV) was investigated. The 1A protein accumulated intracellulary as four species: two species (4.8K and 7.2K) were unglycosylated and differed in length because translational initiation for the synthesis of the 4.8K species occurred at the second methionine in the sequence. The two other forms (13-15K and 21-30K) contained an N-linked carbohydrate side chain. The 13-15K species appeared to be converted into the 21- 30K form by the post-translational additional of polyactosamine to the N-linked side chain. This complex processing pathway for 1A was conserved between the RSV antigenic subgroups. All forms of 1A were shown to be inserted into intracellular membranes regardless of glycosylation status, and all forms except 4.8K were transported to the cell surface. Protein-mapping studies showed that the C-terminus of the 1A protein is extracellular, whereas the N-terminus is cytoplasmic. Additional studies to investigate the structure and processing of other RSV proteins are discussed.

人类小1a蛋白的结构和加工 研究了呼吸综合病毒（RSV）。 1A蛋白 累积的细胞内作为四种：两个物种（4.8K和 7.2k）是未糖基化的，长度有所不同，因为 4.8K物种合成的翻译启动 发生在序列中的第二个蛋氨酸。 另外两个 形式（13-15k和21-30k）包含N连接的碳水化合物侧 链。 13-15k物种似乎已转化为21- 通过后倾斜的多分离胺将30k形式形式 N连接的侧链。 1A的复杂处理途径 在RSV抗原亚组之间保守。 所有形式 1A显示将插入到细胞内膜中 不论糖基化状态如何，除4.8k以外的所有形式都是 运输到细胞表面。 蛋白质图研究显示 1A蛋白的C末端是细胞外的，而 N末端是细胞质。 其他研究以调查 讨论了其他RSV蛋白的结构和处理。