Variation in the affinity of three representative avian adenoviruses for the cellular coxsackievirus and adenovirus receptor
文献类型： 外文期刊
作者： Song, Yapeng 1 ; Tao, Mingyue 1 ; Liu, Lin 1 ; Wang, Yang 1 ; Zhao, Zhenchao 1 ; Huang, Zongmei 1 ; Gao, Wenming 1 ; Wei, Qiang 2 ; Li, Xinsheng 1 ;
作者机构： 1.Henan Agr Univ, Coll Vet Med, Dept Microbiol & Immunol, Zhengzhou, Henan, Peoples R China
2.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China
关键词： Avian adenovirus; fibre; crystal structure; coxsackievirus-adenovirus receptor; affinity variation
期刊名称：VETERINARY RESEARCH （ 影响因子：4.4； 五年影响因子：4.3 ）
ISSN： 0928-4249
年卷期： 2024 年 55 卷 1 期
页码：
收录情况： SCI
摘要： According to previous studies, three representative avian adenoviral strains utilize coxsackievirus-adenovirus receptor (CAR) as a receptor and seem to exhibit diverse binding affinities and modes. Thus, further revealing the exact molecular mechanism underlying the interaction between different FAdVs and the attachment receptor CAR is necessary. In this study, we successfully solved the crystal structure of the FAdV-4 fiber1 knob at 1.6 angstrom resolution. The interaction between the fibre knob and different domains of CAR was verified by confocal microscopy, coimmunoprecipitation and surface plasmon resonance (SPR) analysis. The fibre knobs of the three representative fowl adenoviruses specifically recognized CAR domain 1 (D1), but the recognition of CAR domain 2 (D2) by chicken embryo lethal orphan (CELO) strains was weak. These results provide insights into the differences in adenovirus-host cell interactions and have important implications for the exploration of viral invasion mechanisms.
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