Signaling during pathogen infection

Sci STKE. 2006 May 16;2006(335):re5. doi: 10.1126/stke.3352006re5.

Abstract

Over the millennia, pathogens have coevolved with their hosts and acquired the ability to intercept, disrupt, mimic, and usurp numerous signaling pathways of those hosts. The study of host/pathogen interactions thus not only teaches us about the intricate biology of these parasitic invaders but also provides interesting insights into basic cellular processes both at the level of the individual cell and more globally throughout the organism. Host/pathogen relationships also provide insights into the evolutionary forces that shape biological diversity. Here we review a few recent examples of how viruses, bacteria, and parasites manipulate tyrosine kinase-mediated and Rho guanosine triphosphatase-mediated signaling pathways of their hosts to achieve efficient entry, replication, and exit during their infectious cycles.

Publication types

  • Review

MeSH terms

  • Actin Cytoskeleton / physiology
  • Actins / physiology
  • Animals
  • Cell Adhesion / physiology
  • Cell Line
  • Cell Movement
  • Chlorocebus aethiops
  • Eukaryotic Cells / enzymology*
  • Eukaryotic Cells / microbiology
  • Eukaryotic Cells / parasitology
  • Eukaryotic Cells / virology
  • Female
  • Humans
  • Infections / physiopathology*
  • Intracellular Signaling Peptides and Proteins
  • Malaria / blood
  • Malaria / parasitology
  • Malaria / physiopathology
  • Male
  • Microtubules / physiology
  • Phosphorylation
  • Plasmodium / growth & development
  • Protein Processing, Post-Translational
  • Protein Serine-Threonine Kinases / physiology
  • Protein-Tyrosine Kinases / physiology
  • Signal Transduction*
  • Vaccinia virus / physiology
  • rho GTP-Binding Proteins / physiology
  • rho-Associated Kinases
  • src-Family Kinases / physiology

Substances

  • Actins
  • Intracellular Signaling Peptides and Proteins
  • Protein-Tyrosine Kinases
  • src-Family Kinases
  • Protein Serine-Threonine Kinases
  • rho-Associated Kinases
  • rho GTP-Binding Proteins