Cryo-EM Structure of a Possum Enterovirus

被引：0

作者：

Wang, Ivy ^{[1
]}

Gupta, Sandeep K. ^{[2
]}

Ems, Guillaume ^{[3
,4
]}

Jayawardena, Nadishka ^{[3
,5
]}

Strauss, Mike ^{[1
]}

Bostina, Mihnea ^{[3
,6
]}

机构：

[1] McGill Univ, Dept Anat & Cell Biol, Montreal, PQ H3A 0C7, Canada

[2] AgResearch, Palmerston North 4442, New Zealand

[3] Univ Otago, Dept Microbiol & Immunol, Dunedin 9016, New Zealand

[4] Univ Namur, Fac Sci, B-5000 Namur, Belgium

[5] Okinawa Inst Sci & Technol Grad Univ, Mol Cryoelectron Microscopy Unit, Okinawa 9040495, Japan

[6] Univ Otago, Otago Micro & Nano Imaging, Dunedin 9016, New Zealand

来源：

VIRUSES-BASEL | 2022年 / 14卷 / 02期

基金：

加拿大自然科学与工程研究理事会;

关键词：

enterovirus; possum; capsid structure; cryo-electron microscopy; 3-DIMENSIONAL STRUCTURE; MOLECULAR-BASIS; VIRUS; POLIOVIRUS; PICORNAVIRUS; ATTACHMENT;

D O I：

10.3390/v14020318

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Enteroviruses (EVs) represent a substantial concern to global health. Here, we present the cryo-EM structure of a non-human enterovirus, EV-F4, isolated from the Australian brushtail possum to assess the structural diversity of these picornaviruses. The capsid structure, determined to ~3 angstrom resolution by single particle analysis, exhibits a largely smooth surface, similar to EV-F3 (formerly BEV-2). Although the cellular receptor is not known, the absence of charged residues on the outer surface of the canyon suggest a different receptor type than for EV-F3. Density for the pocket factor is clear, with the entrance to the pocket being smaller than for other enteroviruses.

引用

页数：11

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