| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
* University of Wuerzburg, Research Center for Infectious Diseases, Wuerzburg, Germany;
Department of Anaesthesiology and Intensive Care, Experimental and Clinical Haemostasis, University Hospital Muenster, Muenster, Germany; and
Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Borstel, Germany
2Correspondence: Max von Pettenkofer-Institute for Hygiene and Microbiology, Ludwig-Maximilians University Munich, Pettenkoferstrasse 9a, D-80336 Muenchen, Germany. E-mail: hammerschmidt{at}mvp.uni-muenchen.de
Thrombospondin-1 (TSP1) is a matricellular glycoprotein that has key roles in interactions between human cells and components of the extracellular matrix. Here we report a novel role for the lectin TSP1 in pathogen-host interactions. Binding assays and flow cytometric analysis demonstrate that Streptococcus pneumoniae and other Gram-positive pathogens including S. pyogenes, Staphylococcus aureus, and Listeria monocytogenes interact specifically with human TSP1. We also show for the first time that host cell-bound TSP1 promotes adherence of Gram-positive pathogens to human epithelial and endothelial cell lines. Pretreatment of bacteria with sodium periodate but not Pronase E substantially reduced TSP1-mediated bacterial adherence to host cells, suggesting that a glycoconjugate on the bacterial cell surface functions as the receptor for TSP1. Lipoteichoic acids did not affect TSP1-mediated adherence of S. pneumoniae to host cells. In contrast, attachment of S. pneumoniae and other Gram-positive pathogens to host cells via TSP1 was blocked by soluble peptidoglycan, indicating recognition of bacterial peptidoglycan by TSP1. In conclusion, our results demonstrate that recognition of Gram-positive pathogens by TSP1 promotes bacterial colonization of host tissue cells. In this scenario, peptidoglycan functions as adhesin and TSP1 acts as a molecular bridge linking Gram-positive bacteria with receptors on the host cell.—Rennemeier, C., Hammerschmidt, S., Niemann, S., Inamura, S., Zähringer, U., Kehrel, B. E. Thrombospondin-1 promotes cellular adherence of Gram-positive pathogens via recognition of peptidoglycan.
Key Words: colonization • platelet lectin • pneumococci • staphylococci • host tissue cells
This article has been cited by other articles:
|
|
 |
|
  S. Ribes, S. Ebert, T. Regen, A. Agarwal, S. C. Tauber, D. Czesnik, A. Spreer, S. Bunkowski, H. Eiffert, U.-K. Hanisch, et al. Toll-Like Receptor Stimulation Enhances Phagocytosis and Intracellular Killing of Nonencapsulated and Encapsulated Streptococcus pneumoniae by Murine Microglia Infect. Immun., February 1, 2010; 78(2): 865 - 871. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Noske, U. Kammerer, M. Rohde, and S. Hammerschmidt Pneumococcal Interaction with Human Dendritic Cells: Phagocytosis, Survival, and Induced Adaptive Immune Response Are Manipulated by PavA J. Immunol., August 1, 2009; 183(3): 1952 - 1963. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 V. Agarwal and S. Hammerschmidt Cdc42 and the Phosphatidylinositol 3-Kinase-Akt Pathway Are Essential for PspC-mediated Internalization of Pneumococci by Respiratory Epithelial Cells J. Biol. Chem., July 17, 2009; 284(29): 19427 - 19436. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Bergmann, A. Lang, M. Rohde, V. Agarwal, C. Rennemeier, C. Grashoff, K. T. Preissner, and S. Hammerschmidt Integrin-linked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells J. Cell Sci., January 15, 2009; 122(2): 256 - 267. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
