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首页> 外文期刊>Journal of Molecular Biology >MODIFYING FILAMENTOUS PHAGE CAPSID - LIMITS IN THE SIZE OF THE MAJOR CAPSID PROTEIN
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MODIFYING FILAMENTOUS PHAGE CAPSID - LIMITS IN THE SIZE OF THE MAJOR CAPSID PROTEIN

机译：修改丝状噬菌体的衣壳-主要衣壳蛋白大小的限制

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Ff filamentous phages are long thin cylindrical structures that infect bacteria displaying the F pilus and replicate without lysing the host. These structures are exploited to display peptides by fusing them to the amino terminus of either the bacterial receptor protein (pill) or the major coat protein (pVIII). We have analysed a vast collection of phage mutants containing substitutions and insertions in the amino terminus of pVIII to ask whether any chemical group of this solvent exposed region of the phage capsid has any key function in the phage life cycle. Any of the five amino-terminal residues can be substituted by most amino acids without affecting phage assembly suggesting that this region does not play any essential role in morphogenesis. However, a deletion of three residues Delta(Gly3Asp4Asp5) results in a phage clone with an decreased ability to produce infective particles. By engineering phages designed to display peptides by fusion to the amino terminus of the major coat protein we have found that phage viability is affected by peptide length while peptide sequence plays a minor ''tuning'' role. Most peptides of six residues are tolerated irrespective of their sequence while only 40% of the phages carrying an amino-terminal extension of eight residues can form infective particles. This fraction drops to 20% and 1% when we attempt to insert peptides 10 and 16 amino acids long. We have used this information to build phage libraries where each phage displaysapproximately 2700 copies of a different octapeptide all over the phage surface. [References: 31]
机译：Ff丝状噬菌体是细长的圆柱形结构，可感染显示F菌毛的细菌，并在不裂解宿主的情况下复制。通过将这些结构融合到细菌受体蛋白（药丸）或主要外壳蛋白（pVIII）的氨基末端来利用这些结构来展示肽。我们分析了大量噬菌体突变体，这些噬菌体突变体在pVIII的氨基末端含有取代基和插入物，以询问噬菌体衣壳中该溶剂暴露区域的任何化学基团在噬菌体生命周期中是否具有任何关键功能。五个氨基末端残基中的任何一个都可以被大多数氨基酸取代，而不会影响噬菌体的组装，这表明该区域在形态发生中没有任何重要作用。但是，删除三个残基Delta（Gly3Asp4Asp5）会导致噬菌体克隆产生感染性颗粒的能力降低。通过工程化设计为通过与主要外壳蛋白的氨基末端融合来展示肽的噬菌体，我们发现噬菌体的生存力受肽长度的影响，而肽序列仅起到较小的“调节”作用。无论六个残基的序列如何，大多数肽都是可以耐受的，而携带八个残基的氨基末端延伸的噬菌体中只有40％可以形成感染性颗粒。当我们尝试插入10和16个氨基酸长的肽时，该比例下降到20％和1％。我们已经使用该信息来构建噬菌体文库，其中每个噬菌体在整个噬菌体表面显示大约2700个拷贝的不同八肽。 [参考：31]

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