Revised Mimivirus major capsid protein sequence reveals intron-containing gene structure and extra domain

Saïd Azza1, Christian Cambillau, Didier Raoult

  • 1Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), CNRS-IRD UMR 6236, IFR 48, Faculté de Médecine, 27 Boulevard Jean Moulin, 13385 Marseille cedex 05, France. said.azza@univmed.fr

Abstract

Insights

Researchers characterized the full-length Acanthamoebae polyphaga Mimivirus (APM) major capsid protein and its gene. This study provides new insights into APM structure and aids future viral research.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Acanthamoebae polyphaga Mimivirus (APM) is the largest known double-stranded DNA virus, featuring an icosahedral structure with fibril-covered capsid.
  • The D13L protein, derived from the APM L425 gene, is the most abundant viral particle protein but was poorly characterized.
  • A revised sequence revealed a previously missing N-terminal region, prompting further investigation into the complete APM major capsid protein.

Purpose of the Study:

  • To investigate the L425 gene structure of Acanthamoebae polyphaga Mimivirus (APM).
  • To characterize the biochemical properties of the complete APM major capsid protein.
  • To provide new insights into the structure of the main capsid protein of APM.

Main Methods:

  • Sequencing of the full-length 3430 bp Capsid coding gene (L425).
  • Expression and purification of the recombinant full-length APM Capsid protein 1 (593 amino acids).
  • Production of a specific monoclonal antibody against APM Capsid protein 1.
  • Analysis of post-translational modifications (glycosylation, phosphorylation).
  • Secondary structure prediction and comparison with other Nucleo-Cytoplasmic Large DNA viruses.

Main Results:

  • The full-length L425 gene and the 593 amino acid Capsid protein 1 were characterized.
  • A specific monoclonal antibody confirmed Capsid protein 1's presence within the APM viral particle.
  • Post-translational modifications, including glycosylation and phosphorylation, were identified.
  • A secondary structure prediction for APM Capsid protein 1 was proposed.

Conclusions:

  • Characterization of the full-length L425 gene offers new insights into APM major capsid protein structure.
  • The availability of the full-length recombinant protein facilitates future structural studies of APM.
  • This research enhances understanding of large DNA virus capsid proteins.

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