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


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


    Citations of this article.
  • 1.3k


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


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


  • F Baudin

  • I Petit

  • W Weissenhorn

  • R W Ruigrok

Cite this document

Choose a citation style from the tabs below