Interaction of Trypanosoma evansi with the plasminogen-plasmin system.
Abstract: Trypanosoma evansi is a widely-distributed haemoflagellated parasite of veterinary importance that infects a variety of mammals including horses, mules, camels, buffalos, cattle and deer. It is the causal agent of a trypanosomiasis known as Surra which produces epidemics of great economic importance in Africa, Asia and South America. The main pathology includes an enlarged spleen with hypertrophy of lymphoid follicles, congested lungs, neuronal degeneration and meningoencephalitis, where migration of the parasites from the blood to the tissues is essential. Most cells, including pathogenic cells, use diverse strategies for tissue invasion, such as the expression of surface receptors to bind plasminogen or plasmin. In this work, we show that T. evansi is able to bind plasminogen and plasmin on its surface. The analysis of this binding revealed a high affinity dissociation constant (Kd of 0.080±0.009μM) and 1×10(5) plasminogen binding sites per cell. Also a second population of receptors with a Kd of 0.255±0.070μM and 3.2×10(4) plasminogen binding sites per cell was determined. Several proteins with molecular masses between ∼18 and ∼70kDa are responsible for this binding. This parasite-plasminogen interaction may be important in the establishment of the infection in the vertebrate host, where the physiological concentration of available plasminogen is around 2μM.
Copyright © 2016 Elsevier B.V. All rights reserved.
Publication Date: 2016-07-14 PubMed ID: 27514905DOI: 10.1016/j.vetpar.2016.07.016Google Scholar: Lookup
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Summary
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This research article investigates the interaction between Trypanosoma evansi, a parasite that causes trypanosomiasis in various mammals, and the plasminogen-plasmin system, an important process for tissue invasion in cells. The study found that T. evansi can bind with either plasminogen or plasmin, potentially assisting the migration of the parasite from the blood to the tissues, thereby contributing to the establishment of infection in the host.
Introduction to Trypanosoma evansi and its Impacts
- Trypanosoma evansi is a parasite that commonly infects a wide range of mammals such as horses, mules, camels, buffalos, cattle, and deer.
- The parasite is known to cause trypanosomiasis, also known as Surra, a disease that often leads to serious epidemics in Africa, Asia, and South America.
- Surra majorly impacts the mammals’ health with symptoms such as an enlarged spleen, congested lungs, neuronal degeneration, and meningoencephalitis.
- The infection’s critical aspect lies in the migration of these parasites from the blood to the tissues, especially the lymphoid follicles. This study emphasized on how T. evansi facilitates this process of tissue invasion.
Interaction between T. evansi and Plasminogen-Plasmin System
- Many cells, including pathogenic ones, use sophisticated strategies to invade the tissues. One such common tactic involves the expression of surface receptors that particularly bind with plasminogen or plasmin.
- The study revealed that T. evansi can also bind with either plasminogen or plasmin, signifying its optimized adaptation for tissue invasion.
Analysis of Binding Parameters
- The researchers found a high affinity dissociation constant (Kd) of 0.080±0.009μM and approximately 1×10(5) plasminogen binding sites per cell which indicated a significant correlation between the parasite and plasminogen.
- Further examination unveiled another set of receptors with a Kd of 0.255±0.070μM and 3.2×10(4) plasminogen binding sites per cell.
- Several proteins with molecular masses between ∼18 and ∼70kDa were identified as responsible for this binding.
Potential Implications of the Interaction
- The interaction between the parasite and plasminogen might be a significant factor in the infection’s establishment within the vertebrate host. This is particularly crucial given the fact that the physiological concentration of available plasminogen in such hosts is around 2μM.
- The finding of this study might open new avenues for understanding the mechanisms of infection and ultimately developing more effective treatments for trypanosomiasis.
Cite This Article
APA
Acosta H, Rondón-Mercado R, Avilán L, Concepción JL.
(2016).
Interaction of Trypanosoma evansi with the plasminogen-plasmin system.
Vet Parasitol, 226, 189-197.
https://doi.org/10.1016/j.vetpar.2016.07.016 Publication
Researcher Affiliations
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela. Electronic address: hectoracosta@ula.ve.
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
- Laboratorio de Fisiología Animal. Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
MeSH Terms
- Aminocaproic Acid / metabolism
- Animals
- Binding Sites
- Carbonates / pharmacology
- Cell Membrane / metabolism
- Fibrinolysin / metabolism
- Fluorescent Antibody Technique
- Horses
- Immune Sera / immunology
- Microsomes / chemistry
- Microsomes / drug effects
- Plasminogen / immunology
- Plasminogen / metabolism
- Protozoan Proteins / analysis
- Rabbits
- Rats
- Rats, Wistar
- Receptors, Cell Surface / metabolism
- Trypanosoma / metabolism
- Trypanosoma / pathogenicity
- Trypanosoma / physiology
- Trypanosomiasis / parasitology
- Trypanosomiasis / pathology
- Trypanosomiasis / veterinary
- Tubulin / immunology
- Urokinase-Type Plasminogen Activator / metabolism
Citations
This article has been cited 3 times.- Pala ZR, Ernest M, Sweeney B, Jeong YJ, Pascini TV, Alves E Silva TL, Vega-Rodríguez J. Beyond cuts and scrapes: plasmin in malaria and other vector-borne diseases. Trends Parasitol 2022 Feb;38(2):147-159.
- Diosdado A, Simón F, Morchón R, González-Miguel J. Pro-fibrinolytic potential of the third larval stage of Ascaris suum as a possible mechanism facilitating its migration through the host tissues. Parasit Vectors 2020 Apr 20;13(1):203.
- Ayón-Núñez DA, Fragoso G, Bobes RJ, Laclette JP. Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases. Biosci Rep 2018 Oct 31;38(5).
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