Refinement and Analysis of the Mature Zika Virus Cryo-EM Structure at 3.1 Å Resolution

被引：70

作者：

Sevvana, Madhumati ^{[1
]}

Long, Feng ^{[1
]}

Miller, Andrew S. ^{[1
]}

Klose, Thomas ^{[1
]}

Buda, Geeta ^{[1
]}

Sun, Lei ^{[1
,2
,3
]}

Kuhn, Richard J. ^{[1
]}

Rossmann, Michael G. ^{[1
]}

机构：

[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA

[2] Fudan Univ, Peoples Hosp Shanghai 5, Shanghai, Peoples R China

[3] Fudan Univ, Inst Biomed Sci, Shanghai, Peoples R China

来源：

STRUCTURE | 2018年 / 26卷 / 09期

关键词：

BORNE ENCEPHALITIS-VIRUS; WEST-NILE-VIRUS; DENGUE VIRUS; CRYOELECTRON MICROSCOPY; FAB FRAGMENTS; MATURATION; IMMATURE; ANTIBODY; NEUTRALIZATION; COMPLEX;

D O I：

10.1016/j.str.2018.05.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Among the several arthropod-borne human flaviviral diseases, the recent outbreak of Zika virus (ZIKV) has caused devastating birth defects and neurological disorders, challenging the world with another major public health concern. We report here the refined structure of the mature ZIKV at a resolution of 3.1 angstrom as determined by cryo-electron microscopic single-particle reconstruction. The improvement in the resolution, compared with previous enveloped virus structures, was the result of optimized virus preparation methods and data processing techniques. The glycoprotein interactions and surface properties of ZIKV were compared with other mosquito-borne flavivirus structures. The largest structural differences and sequence variations occur at the glycosylation loop associated with receptor binding. Probable drug binding pockets were identified on the viral surface. These results also provide a structural basis for the design of vaccines against ZIKV.

引用

页码：1169 / +

页数：12

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