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Structure of the AAVhu.37 capsid by cryoelectron microscopy.
Acta Crystallographica Section F ( IF 1.072 ) Pub Date : 2020-02-10 , DOI: 10.1107/s2053230x20000308
Jason T Kaelber 1 , Samantha A Yost 2 , Keith A Webber 3 , Emre Firlar 1 , Ye Liu 2 , Olivier Danos 2 , Andrew C Mercer 2
Affiliation  

Adeno‐associated viruses (AAVs) are used as in vivo gene‐delivery vectors in gene‐therapy products and have been heavily investigated for numerous indications. Over 100 naturally occurring AAV serotypes and variants have been isolated from primate samples. Many reports have described unique properties of these variants (for instance, differences in potency, target cell or evasion of the immune response), despite high amino‐acid sequence conservation. AAVhu.37 is of interest for clinical applications owing to its proficient transduction of the liver and central nervous system. The sequence identity of the AAVhu.37 VP1 to the well characterized AAVrh.10 serotype, for which no structure is available, is greater than 98%. Here, the structure of the AAVhu.37 capsid at 2.56 Å resolution obtained via single‐particle cryo‐electron microscopy is presented.

中文翻译:

通过冷冻电子显微镜观察 AAVhu.37 衣壳的结构。

腺相关病毒(AAV)在基因治疗产品中用作体内基因传递载体,并已针对多种适应症进行了深入研究。已从灵长类动物样本中分离出 100 多种天然存在的 AAV 血清型和变种。尽管氨基酸序列高度保守,但许多报告描述了这些变体的独特特性(例如,效力、靶细胞或逃避免疫反应的差异)。AAVhu.37 由于其对肝脏和中枢神经系统的熟练转导而受到临床应用的关注。AAVhu.37 VP1 与已充分表征的 AAVrh.10 血清型(尚无可用结构)的序列同一性大于 98%。这里展示了通过单颗粒冷冻电子显微镜获得的分辨率为 2.56 Å 的 AAVhu.37 衣壳的结构。
更新日期:2020-02-10
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