School of Nursing, Johns Hopkins University, Baltimore, MD 21205, USA.
Department of Microbiology and Immunology, Tulane University School of Medicine, New Orleans, LA 70112, USA.
Viruses. 2019 Aug 14;11(8):750. doi: 10.3390/v11080750.
A metatranscriptomic study of RNA viruses in cold-blooded vertebrates identified two related viruses from frogfish () that represent a new genus in the family (Order: ). Computational analyses were used to identify features common to class I viral fusion proteins (VFPs) in antennavirus glycoproteins, including an N-terminal fusion peptide, two extended alpha-helices, an intrahelical loop, and a carboxyl terminal transmembrane domain. Like mammarenavirus and hartmanivirus glycoproteins, the antennavirus glycoproteins have an intracellular zinc-binding domain and a long virion-associated stable signal peptide (SSP). The glycoproteins of reptarenaviruses are also class I VFPs, but do not contain zinc-binding domains nor do they encode SSPs. Divergent evolution from a common progenitor potentially explains similarities of antennavirus, mammarenavirus, and hartmanivirus glycoproteins, with an ancient recombination event resulting in a divergent reptarenavirus glycoprotein.
对冷血脊椎动物的 RNA 病毒的宏转录组学研究，从蓑鲉中鉴定出两种相关病毒，它们代表了 科（目：）中的一个新属。通过计算分析，确定了触角病毒糖蛋白中 I 类病毒融合蛋白（VFP）的共有特征，包括 N 端融合肽、两个扩展的α螺旋、一个内环、和一个羧基末端跨膜结构域。与哺乳动物病毒和哈特曼病毒糖蛋白一样，触角病毒糖蛋白具有细胞内锌结合域和长的病毒相关稳定信号肽（SSP）。爬行动物病毒的糖蛋白也是 I 类 VFP，但不包含锌结合域，也不编码 SSP。从共同祖先的分歧进化可能解释了触角病毒、哺乳动物病毒和哈特曼病毒糖蛋白的相似性，一个古老的重组事件导致了分歧的爬行动物病毒糖蛋白。
