Europe PMC
[go: up one dir, main page]

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our privacy notice and cookie policy.

Cryo-EM structure of a herpesvirus capsid at 3.1 Å.

Author information

Affiliations

  • 1. National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
      Authors
    • Yuan S 1
    • Wang J 1
    • Zhu D 1
    • Wang N 1
    • Gao Q 1
    • Zhang X 1
    • Rao Z 1
    • Wang X 1
    (8 authors)
  • 2. College of Physics and Information Science, Synergetic Innovation Center for Quantum Effects and Applications, Hunan Normal University, Changsha, 410081, Hunan, China.
      Authors
    • Chen W 2
    • Tang H 2
    • Liu H 2
    (3 authors)
  • 3. National Institutes for Food and Drug Control, No. 2, Tiantanxili, Beijing, 100050, China.
      Authors
    • Wang J 3
    (1 author)

ORCIDs linked to this article

Show all (9)

Science, 01 Apr 2018, 360(6384):eaao7283
https://doi.org/10.1126/science.aao7283 PMID: 29622627 

Abstract 

Structurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we report the herpes simplex virus type 2 (HSV-2) capsid structure at 3.1 angstroms, which is built up of about 3000 proteins organized into three types of hexons (central, peripentonal, and edge), pentons, and triplexes. Both hexons and pentons contain the major capsid protein, VP5; hexons also contain a small capsid protein, VP26; and triplexes comprise VP23 and VP19C. Acting as core organizers, VP5 proteins form extensive intermolecular networks, involving multiple disulfide bonds (about 1500 in total) and noncovalent interactions, with VP26 proteins and triplexes that underpin capsid stability and assembly. Conformational adaptations of these proteins induced by their microenvironments lead to 46 different conformers that assemble into a massive quasisymmetric shell, exemplifying the structural and functional complexity of HSV.

Full text links 

Read article at publisher's site: https://doi.org/10.1126/science.aao7283

Read article for free, from open access legal sources, via Unpaywall: https://science.sciencemag.org/content/sci/360/6384/eaao7283.full.pdfUnpaywall

References 

Articles referenced by this article (69)

Show 10 more references (10 of 69)

Citations & impact 

Impact metrics

57
Citations
Jump to Citations
6
Data citations
Jump to Data

Citations of article over time

Alternative metrics

Altmetric item for https://www.altmetric.com/details/35581971
Altmetric
Discover the attention surrounding your research
https://www.altmetric.com/details/35581971

Smart citations by scite.ai
Smart citations by scite.ai include citation statements extracted from the full text of the citing article. The number of the statements may be higher than the number of citations provided by EuropePMC if one paper cites another multiple times or lower if scite has not yet processed some of the citing articles.
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1126/science.aao7283

Supporting
Mentioning
Contrasting
6
122
1

Article citations

Go to all (57) article citations

Data 

Data behind the article

This data has been text mined from the article, or deposited into data resources.

Electron Microscopy Data Bank (EMDB) at PDBe

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.

Funding 

Funders who supported this work.

National Science Foundation of China (1)

the 973 Projects (1)

the National Key Research and Development Program of MOST (1)

the Strategic Priority Research Program (1)