Enteric adenoviruses, one of the main causes of viral gastroenteritis in the world, must withstand the harsh conditions found in the gut. This requirement suggests that capsid stability must be different from that of other adenoviruses. We report the 4-Å-resolution structure of a human enteric adenovirus, HAdV-F41, and compare it with that of other adenoviruses with respiratory (HAdV-C5) and ocular (HAdV-D26) tropisms. While the overall structures of hexon, penton base, and internal minor coat proteins IIIa and VIII are conserved, we observe partially ordered elements reinforcing the vertex region, which suggests their role in enhancing the physicochemical capsid stability of HAdV-F41. Unexpectedly, we find an organization of the external minor coat protein IX different from all previously characterized human and nonhuman mastadenoviruses. Knowledge of the structure of enteric adenoviruses provides a starting point for the design of vectors suitable for oral delivery or intestinal targeting.

肠道腺病毒是世界上病毒性肠胃炎的主要原因之一，必须承受肠道中的恶劣条件。这一要求表明衣壳稳定性必须不同于其他腺病毒。我们报告了人类肠道腺病毒 HAdV-F4​​1 的 4-Å 分辨率结构，并将其与其他具有呼吸道 (HAdV-C5) 和眼 (HAdV-D26) 嗜性的腺病毒进行了比较。虽然六邻体、五邻体碱基和内部次要外壳蛋白 IIIa 和 VIII 的整体结构是保守的，但我们观察到部分有序的元素增强了顶点区域，这表明它们在增强 HAdV-F4​​1 的物理化学衣壳稳定性中的作用。出乎意料的是，我们发现外部次要外壳蛋白 IX 的组织不同于所有先前表征的人类和非人类乳腺病毒。