Seeing the Herpesvirus Capsid at 8.5 Å-Reference-Cited by-同舟云学术

Seeing the Herpesvirus Capsid at 8.5 Å

Published:2000-05-05 Issue:5467 Volume:288 Page:877-880
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Zhou Z. Hong¹,Dougherty Matthew²,Jakana Joanita²,He Jing³,Rixon Frazer J.⁴,Chiu Wah²³

Affiliation:

1. Department of Pathology and Laboratory Medicine, University of Texas–Houston Medical School, Houston, TX 77030, USA.

2. National Center for Macromolecular Imaging, Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.

3. Graduate Program in Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.

4. MRC Virology Unit, Institute of Virology, Glasgow G11 5JR, Scotland, UK.

Abstract

Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative α helices were identified in the four proteins that make up the 0.2 billion–dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference36 articles.

1. B. N. Fields et al. Eds. Fields Virology (Lippincott-Raven Philadelphia 1996) vol. 2.

2. B. N. Roizman and A. E. Sears in (1) pp. 2231–2295; R. J. Whitley in (1) pp. 2297–2342; W. J. Britt and C. A. Alford in (1) pp. 2493–2524; A. M. Arvin in (1) pp. 2547–2586; A. B. Rickinson and E. Kieff in (1) pp. 2397–2446; T. F. Schulz Y. Chang P. S. Moore in Human Tumor Viruses D. J. McCance Ed. (American Society for Microbiology Press Washington DC 1998) pp. 87–134.

3. A. C. Steven and P. G. Spear in Structural Biology of Viruses W. Chiu R. M. Burnett R. L. Garcea Eds. (Oxford Univ. Press New York 1997) pp. 312–351.

4. Microtubule-mediated Transport of Incoming Herpes Simplex Virus 1 Capsids to the Nucleus

5. Batterson W., Furlong D., Roizman B., J. Virol. 45, 397 (1983).

Cited by 272 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. STT3A-mediated viral N-glycosylation underlies the tumor selectivity of oncolytic virus M1;Oncogene;2023-10-20

2. Signals are required by HSV-1 infected neurons to increase the amount of Aβ protein in the brain of Alzheimer’s disease patients;Biophysical Society of GuangDong Province Academic Forum: Precise Photons and Life Health (PPLH 2022);2023-04-04

3. Creating Artificial Viruses Using Self-assembled Proteins and Polypeptides;Physical Virology;2023

4. Soft X-ray Tomography Reveals HSV-1-Induced Remodeling of Human B Cells;Viruses;2022-11-27

5. Exact Solution for Elastic Networks on Curved Surfaces;Physical Review Letters;2022-08-17