Skip to content
Journal article

In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.

Baudin F, Petit I, Weissenhorn W, Ruigrok R ...see all

Virology, vol. 281, issue 1 (2001) pp. 102-108

  • 72

    Readers

    Mendeley users who have this article in their library.
  • 98

    Citations

    Citations of this article.
  • 1.3k

    Views

    ScienceDirect users who have downloaded this article.
Sign in to save reference

Abstract

Spontaneous proteolysis of influenza virus M1 protein during crystallisation has defined an N-terminal domain of amino acids 1--164. Full-length M1, the N-terminal domain, and the C-terminal part of M1 (residues 165--252) were produced in Escherichia coli. In vitro tests showed that only full-length M1 and its N-terminal domain bind to negatively charged liposomes and that only full-length M1 and its C-terminal part bind to RNP. However, only full-length M1 had transcription inhibition activity. Several independent experimental approaches indicate that in vitro transcription inhibition occurs through polymerisation/aggregation of M1 onto RNP, or of M1 onto M1 already bound to RNP, rather than by binding to a specific active site on the nucleoprotein or the polymerase. The structure/function of influenza virus M1 will be compared with that of the Ebola virus matrix protein, VP40.

Author-supplied keywords

  • Ebolavirus
  • Ebolavirus: chemistry
  • Electron
  • Genetic
  • Liposomes
  • Liposomes: metabolism
  • Microscopy
  • Mutation
  • Mutation: genetics
  • Nuclear Localization Signals
  • Nuclear Localization Signals: genetics
  • Orthomyxoviridae
  • Orthomyxoviridae: chemistry
  • Peptide Fragments
  • Peptide Fragments: chemistry
  • Peptide Fragments: genetics
  • Peptide Fragments: metabolism
  • Protein Binding
  • Protein Structure
  • Ribonucleoproteins
  • Ribonucleoproteins: chemistry
  • Ribonucleoproteins: genetics
  • Ribonucleoproteins: metabolism
  • Ribonucleoproteins: ultrastructure
  • Sodium Chloride
  • Sodium Chloride: pharmacology
  • Solubility
  • Solubility: drug effects
  • Static Electricity
  • Tertiary
  • Transcription
  • Viral Matrix Proteins
  • Viral Matrix Proteins: chemistry
  • Viral Matrix Proteins: genetics
  • Viral Matrix Proteins: metabolism
  • Viral Matrix Proteins: ultrastructure
  • influenza virus
  • m1
  • m1 protein
  • membrane interaction
  • rnp interaction
  • transcription inhibition

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text

Authors

  • F Baudin

  • I Petit

  • W Weissenhorn

  • R W Ruigrok

Cite this document

Choose a citation style from the tabs below