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Streptococcus pyogenes M49 plasminogen/plasmin binding facilitates keratinocyte invasion via integrin-integrin-linked kinase (ILK) pathways and protects from macrophage killing
- Source :
- The Journal of biological chemistry. 286(24)
- Publication Year :
- 2011
-
Abstract
- The entry into epithelial cells and the prevention of primary immune responses are a prerequisite for a successful colonization and subsequent infection of the human host by Streptococcus pyogenes (group A streptococci, GAS). Here, we demonstrate that interaction of GAS with plasminogen promotes an integrin-mediated internalization of the bacteria into keratinocytes, which is independent from the serine protease activity of potentially generated plasmin. α(1)β(1)- and α(5)β(1)-integrins were identified as the major keratinocyte receptors involved in this process. Inhibition of integrin-linked kinase (ILK) expression by siRNA silencing or blocking of PI3K and Akt with specific inhibitors, reduced the GAS M49-plasminogen/plasmin-mediated invasion of keratinocytes. In addition, blocking of actin polymerization significantly reduced GAS internalization into keratinocytes. Altogether, these results provide a first model of plasminogen-mediated GAS invasion into keratinocytes. Furthermore, we demonstrate that plasminogen binding protects the bacteria against macrophage killing.
- Subjects :
- Keratinocytes
Integrins
Plasmin
Streptococcus pyogenes
media_common.quotation_subject
Integrin
Protein Serine-Threonine Kinases
medicine.disease_cause
Biochemistry
Models, Biological
Integrin alpha1beta1
Bacteriocins
Cell Line, Tumor
medicine
Cell Adhesion
Humans
Integrin-linked kinase
Fibrinolysin
Internalization
Molecular Biology
Protein kinase B
PI3K/AKT/mTOR pathway
media_common
biology
Models, Genetic
Macrophages
Cell Biology
Molecular biology
medicine.anatomical_structure
biology.protein
Keratinocyte
Peptides
medicine.drug
Integrin alpha5beta1
Protein Binding
Signal Transduction
Subjects
Details
- ISSN :
- 1083351X
- Volume :
- 286
- Issue :
- 24
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....95dd0572fa081dcf04a96a6eecbb8fc6