Structure of the chlorovirus PBCV-1 major capsid glycoprotein determined by combining crystallographic and carbohydrate molecular modeling approaches

Cristina De Castro, Thomas Klose, Immacolata Speciale, Rosa Lanzetta, Antonio Molinaro, James L. Van Etten, Michael G. Rossmann

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

,, The glycans of the major capsid protein (Vp54) of Paramecium bursaria chlorella virus (PBCV-1) were recently described and found to be unusual. This prompted a reexamination of the previously reported Vp54 X-ray structure. A detailed description of the complete glycoprotein was achieved by combining crystallographic data with molecular modeling. The crystallographic data identified most of the monosaccharides located close to the protein backbone, but failed to detect those further from the glycosylation sites. Molecular modeling complemented this model by adding the missing monosaccharides and examined the conformational preference of the whole molecule, alone or within the crystallographic environment. Thus, combining X-ray crystallography with carbohydrate molecular modeling resulted in determining the complete glycosylated structure of a glycoprotein. In this case, it is the chlorovirus PBCV-1 major capsid protein.

Original languageEnglish (US)
Pages (from-to)E44-E52
JournalProceedings of the National Academy of Sciences of the United States of America
Volume115
Issue number1
DOIs
StatePublished - Jan 2 2018

Keywords

  • Capsid protein
  • Chloroviruses
  • Glycoprotein structure
  • N-glycans
  • Virus PBCV-1

ASJC Scopus subject areas

  • General

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