Publications by authors named "Amaranta Gomez-Arreaza"

The complex parasite-host relationship involves multiple mechanisms. Moreover, parasites infected by viruses modify this relationship adding more complexity to the system that now comprises three partners. Viruses infecting parasites were described several decades ago.

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Article Synopsis
  • Glycolytic enzymes, typically found inside cells for carbohydrate and energy metabolism, have been discovered in extracellular locations in many organisms, especially pathogens.
  • These enzymes can be secreted or attached to parasite surfaces, performing additional functions, known as "moonlighting," such as interacting with host components.
  • They play crucial roles in parasite-host interactions, aiding in adherence, invasion, immune modulation, nutrient acquisition, and overall virulence of the parasites.
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The interaction of pathogenic bacteria with the host fibrinolytic system through the plasminogen molecule has been well documented. It has been shown, using animal models, to be important in invasion into the host and establishment of the infection. From a number of recent observations with parasitic protists and helminths, emerges evidence that also in these organisms the interaction with plasminogen may be important for infection and virulence.

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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.

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Leishmania mexicana is able to interact with the fibrinolytic system through its component plasminogen, the zymogenic form of the protease plasmin. In this study a new plasminogen binding protein of this parasite was identified: LACK, the Leishmania homolog of receptors for activated C-kinase. Plasminogen binds recombinant LACK with a K(d) value of 1.

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