Abstract
Membrane vesicles secreted by Leishmania mexicana were collected and analyzed. These vesicles can bind plasminogen and were shown to contain enolase, previously identified as a plasminogen-binding protein. In addition, another plasminogen-binding protein was identified, the small myristoylated protein, SMP-1. Recombinant SMP-1 was able to bind plasminogen in a lysine-dependent manner with a K(d) value of 0.24 μM. The C-terminal lysine seems to be responsible for this binding, since this recognition decreases upon carboxypeptidase B treatment. This protein was present within the secreted membrane vesicles as demonstrated by its protection from trypsin digestion in the absence of Triton X-100. Plasminogen-binding proteins in the secreted vesicles may be involved in parasite invasion in the mammalian host.
| Original language | English |
|---|---|
| Pages (from-to) | 14-20 |
| Number of pages | 7 |
| Journal | Molecular and Biochemical Parasitology |
| Volume | 187 |
| Issue number | 1 |
| Early online date | 22 Nov 2012 |
| DOIs | |
| Publication status | Published - Jan 2013 |
Keywords
- Host-Pathogen Interactions
- Kinetics
- Leishmania mexicana/metabolism
- Lysine/metabolism
- Plasminogen/metabolism
- Protein Binding
- Protozoan Proteins/metabolism
- Secretory Vesicles/metabolism
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