Structural analysis of peptides that interact with Newcastle disease virus
Structural analysis of peptides that interact with Newcastle disease virus
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DOI：
10.1016/j.peptides.2005.11.018
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发表时间：
2006-06-01
期刊：
影响因子：
3
通讯作者：
Satyanarayanajois, Seetharama D.
中科院分区：
文献类型：
--
作者：
Chia, Suet Lin;Tan, Wen Siang;Satyanarayanajois, Seetharama D.
一种序列为CTLTTKLYC的肽在鸡胚蛋和组织培养物中抑制新城疫病毒（NDV）的繁殖。根据NDV的解离常数，将NDV分为两大类：速生型和中生型，另一类是慢生型菌株。本研究合成并突变了丝状M13噬菌体pIII蛋白上显示的肽CTLTTKLYC，以鉴定与NDV相互作用相关的氨基酸残基。C1和K6对A1和A6的突变对结合没有明显影响，但用A8取代Y8显著降低了相互作用。这表明Y8在多肽-病毒相互作用中起重要作用。利用圆二色性（CD）、核磁共振（NMR）和分子模型确定了肽的三维结构。肽具有两种可能的构象。由T2-L3-T4-T5和K6-L7-Y8C9组成的连续的β旋转另一种构象在L3-T4-T5-K6周围呈β -发夹弯曲型结构。(c) 2005爱思唯尔公司版权所有。
A peptide with the sequence CTLTTKLYC has previously been identified to inhibit the propagation of Newcastle disease virus (NDV) in embryonated chicken eggs and tissue culture. NDV has been classified into two main groups: the velogenic group, and mesogenic with lentogenic strains as the other group based on its dissociation constants. In this study the peptide, CTLTTKLYC, displayed on the pIII protein of a filamentous M13 phage was synthesized and mutated in order to identify the amino acid residues involved in the interactions with NDV. Mutations of C1 and K6 to A1 and A6 did not affect the binding significantly, but substitution of Y8 with A8 dramatically reduced the interaction. This suggests that Y8 plays an important role in the peptide-virus interaction. The three-dimensional structure of the peptide was determined using circular dichroism (CD), nuclear magnetic resonance (NMR), and molecular modeling. The peptide exhibited two possible conformers. One that consists of consecutive beta-turns around T2-L3-T4-T5 and K6-L7-Y8C9. The other conformer exhibited a beta-hairpin bend type of structure with a bend around L3-T4-T5-K6. (c) 2005 Elsevier Inc. All rights reserved.