Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A

EMBO J. 1995 Mar 1;14(5):894-907.


Poliovirus RNA replication occurs on the surface of membranous vesicles that proliferate throughout the cytoplasm of the infected cell. Since at least some of these vesicles are thought to originate within the secretory pathway of the host cell, we examined the effect of poliovirus infection on protein transport through the secretory pathway. We found that transport of both plasma membrane and secretory proteins was inhibited by poliovirus infection early in the infectious cycle. Transport inhibition did not require viral RNA replication or the inhibition of host cell translation by poliovirus. The viral proteins 2B and 3A were each sufficient to inhibit transport in the absence of viral infection. The intracellular localization of a secreted protein in the presence of 3A with the endoplasmic reticulum suggested that 3A directly blocks transport from the endoplasmic reticulum to the Golgi apparatus.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cell Line
  • Cell Membrane Permeability
  • Cytoplasm / chemistry
  • Endocytosis
  • Endoplasmic Reticulum / metabolism
  • Glycosylation
  • Golgi Apparatus / metabolism
  • Humans
  • Hygromycin B / metabolism
  • Hygromycin B / pharmacology
  • Isomerases / analysis
  • Membrane Glycoproteins*
  • Plasmids
  • Poliovirus / metabolism*
  • Protein Biosynthesis / drug effects
  • Protein Disulfide-Isomerases
  • RNA, Viral / biosynthesis
  • Recombinant Fusion Proteins / metabolism
  • Transfection
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism*
  • Viral Nonstructural Proteins / physiology*
  • alpha 1-Antitrypsin / genetics
  • alpha 1-Antitrypsin / metabolism*


  • G protein, vesicular stomatitis virus
  • Membrane Glycoproteins
  • RNA, Viral
  • Recombinant Fusion Proteins
  • Viral Envelope Proteins
  • Viral Nonstructural Proteins
  • alpha 1-Antitrypsin
  • Hygromycin B
  • Isomerases
  • Protein Disulfide-Isomerases