Medical Journals

Membrane Rafts in Host-pathogen Interactions.

Authors:
  • Riethmüller Joachim
  • Riehle Andrea
  • Grassmé Heike
  • Gulbins Erich

From: Children’s Hospital, University of Tuebingen, Hoppe-Seyler Str. 1, 72076 Tuebingen, Germany.

Biochimica et biophysica acta

  • Publish Date: Dec 2006
  • ISSN: 0006-3002
  • Volume: 1758
  • Issue: 12
  • Pages: 2139-47
  • Medium: Print
  • Language: English
  • Citation (JAMA): Riethmüller Joachim, Riehle Andrea, Grassmé Heike, et al. Membrane Rafts in Host-pathogen Interactions.. Biochim. Biophys. Acta Dec 2006;1758:2139-47

Abstract

Central elements in the infection of mammalian cells with viral, bacterial and parasitic pathogens include the adhesion of the pathogen to surface receptors of the cell, recruitment of additional receptor proteins to the infection-site, a re-organization of the membrane and, in particular, the intracellular signalosome. Internalization of the pathogen results in the formation of a phagosome that is supposed to fuse with lysosomes to form phagolysosomes, which serve the degradation of the pathogen, an event actively prevented by some pathogens. In summary, these changes in the infected cell permit pathogens to trigger apoptosis (for instance of macrophages paralysing the initial immune response), to invade the cell and/or to survive in the cell, but they also serve the mammalian cell to defeat the infection, for instance by activation of transcription factors and the release of cytokines. Distinct membrane domains in the plasma membrane and intracellular vesicles that are mainly composed of sphingolipids and cholesterol or enriched with the sphingolipid ceramide, are critically involved in all of these events occurring during the infection. These membrane structures are therefore very attractive targets for novel drugs to interfere with bacterial, viral and parasitic infections.

Mesh Headings (Keywords): Animals, Bacteria, Bacterial Physiology, HIV, Humans, Membrane Lipids, Plasmodium falciparum, Prion Diseases


Check for Full Text / PubMed Unique Identifier (PMID): 17094939


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.

The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


Advertisements

About | Privacy Policy | Business Solutions | Advertise | Contact | Add Healia to your site

©2012. Healia / Meredith Corporation  

Use of this site constitutes acceptance of our Terms of Service and Privacy Policy. All content on this Web site, including medical opinion and any other health-related information, is for informational purposes only and should not be used for a specific diagnosis or individual treatment plan for any situation. Use of this site and the information contained herein does not create a doctor-patient relationship. Always seek the direct advice of your doctor in connection with any questions or issues you may have regarding your own health or the health of others.