Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host.
Research output: Contribution to journal › Article
Laminin (Ln) and collagen are multifunctional glycoproteins that play an important role in cellular morphogenesis, cell signaling, tissue repair and cell migration. These proteins are ubiquitously present in tissues as a part of the basement membrane (BM), constitute a protective layer around blood capillaries, and are included in the extracellular matrix (ECM). As a component of BMs, both Lns and collagen(s) are found in the blood-brain barrier, and thus function as major mechanical containment molecules that protect tissues from pathogens. Invasive pathogens breach the basal lamina and degrade ECM proteins of interstitial spaces and connective tissues by using various ECM degrading proteases or surface-bound plasminogen and matrix metalloproteinases recruited from the host. Most pathogens associated with the respiratory, gastrointestinal, or urogenital tracts, as well as the CNS or the skin have the capacity to bind and degrade Lns and collagen(s) in order to adhere to and invade host tissues. In this review we focus on the adaptability of various pathogens to utilize these ECM proteins as enhancers for adhesion to host tissues or as a targets for degradation in order to breach the cellular barriers. The major pathogens discussed are Streptococcus, Staphylococcus, Pseudomonas, Salmonella, Yersinia, Treponema, Mycobacterium, Clostridium, Listeria, Porphyromonas and Haemophilus; Candida, Aspergillus, Pneumocystis, Cryptococcus and Coccidioides; Acanthamoeba, Trypanosoma and Trichomonas; Retrovirus and papilloma virus © 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.
|Research areas and keywords||
Subject classification (UKÄ) – MANDATORY
|Journal||FEMS Microbiology Reviews|
|Publication status||Published - 2012|