Skehel J J, Cross K, Steinhauer D, Wiley D C
Division of Virology, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
Biochem Soc Trans. 2001 Aug;29(Pt 4):623-6. doi: 10.1042/bst0290623.
The 'fusion peptides' of a group of enveloped viruses that includes influenza, paramyxo-, retro-and filo-viruses are N-terminal regions of their membrane fusion proteins generated by cleavage of non-functional precursors. For the influenza membrane fusion protein, haemagglutinin (HA), the three-dimensional structures of precursor HA, cleaved HA and fusion-activated HA show that the fusion peptides are located in different positions in all three forms and adopt different structures. Analyses of mutant HAs with changes in fusion peptide sequence indicate the importance of specific residues for membrane-fusion activity and suggest a structure for the fusion peptide in a fusion-active molecule.
包括流感病毒、副粘病毒、逆转录病毒和丝状病毒在内的一组包膜病毒的“融合肽”是其膜融合蛋白的N端区域,由无功能前体的切割产生。对于流感病毒的膜融合蛋白血凝素(HA),前体HA、切割后的HA和融合激活后的HA的三维结构表明,融合肽在这三种形式中处于不同位置,并采用不同结构。对融合肽序列发生变化的突变型HA的分析表明特定残基对膜融合活性的重要性,并提示了融合活性分子中融合肽的结构。