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Capsid protein identification and analysis of mature Triatoma virus (TrV) virions and naturally occurring empty particles

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Published copy (DOI)

Author(s)

  • Jon Agirre
  • Kerman Aloria
  • Jesus M Arizmendi
  • Ibón Iloro
  • Félix Elortza
  • Rubén Sánchez-Eugenia
  • Gerardo A Marti
  • Emmanuelle Neumann
  • Félix A Rey
  • Diego M A Guérin

Department/unit(s)

Publication details

JournalVIROLOGY
DatePublished - 5 Jan 2011
Issue number1
Volume409
Number of pages11
Pages (from-to)91-101
Original languageEnglish

Abstract

Triatoma virus (TrV) is a non-enveloped +ssRNA virus belonging to the insect virus family Dicistroviridae. Mass spectrometry (MS) and gel electrophoresis were used to detect the previously elusive capsid protein VP4. Its cleavage sites were established by sequencing the N-terminus of the protein precursor and MS, and its stoichiometry with respect to the other major capsid proteins (VP1-3) was found to be 1:1. We also characterized the polypeptides comprising the naturally occurring non-infectious empty capsids, i.e., RNA-free TrV particles. The empty particles were composed of VP0-VP3 plus at least seven additional polypeptides, which were identified as products of the capsid precursor polyprotein. We conclude that VP4 protein appears as a product of RNA encapsidation, and that defective processing of capsid proteins precludes genome encapsidation.

    Research areas

  • Animals, Capsid, Capsid Proteins, Dicistroviridae, Electrophoresis, Agar Gel, Mass Spectrometry, Microscopy, Electron, Transmission, Triatoma, Virion, Virus Assembly

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