Crystal structure of Marburg virus VP24.

Adrianna P P Zhang, Zachary A Bornholdt, Dafna M Abelson, Erica Ollmann Saphire
Author Information
  1. Adrianna P P Zhang: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.

Abstract

The VP24 protein plays an essential, albeit poorly understood role in the filovirus life cycle. VP24 is only 30% identical between Marburg virus and the ebolaviruses. Furthermore, VP24 from the ebolaviruses is immunosuppressive, while that of Marburg virus is not. The crystal structure of Marburg virus VP24, presented here, reveals that although the core is similar between the viral genera, Marburg VP24 is distinguished by a projecting β-shelf and an alternate conformation of the N-terminal polypeptide.

Associated Data

PDB | 4OR8

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Grants

  1. T32 AI007244/NIAID NIH HHS
  2. 5P32 AI007244/NIAID NIH HHS

MeSH Term

Crystallography, X-Ray
Models, Molecular
Protein Conformation
Viral Proteins

Chemicals

VP24 protein, Marburg virus
Viral Proteins

Word Cloud

Created with Highcharts 10.0.0VP24Marburgvirusebolavirusesstructureproteinplaysessentialalbeitpoorlyunderstoodrolefiloviruslifecycle30%identicalFurthermoreimmunosuppressivecrystalpresentedrevealsalthoughcoresimilarviralgeneradistinguishedprojectingβ-shelfalternateconformationN-terminalpolypeptideCrystal

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