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Luisana Avilán - One of the best experts on this subject based on the ideXlab platform.
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Plasminogen binding proteins in secreted membrane vesicles of Leishmania mexicana.
Molecular and Biochemical Parasitology, 2012Co-Authors: Lourdes Figuera, Wilfredo Quinones, Juan Luis Concepcion, Héctor Acosta, Amaranta Gómez-arreaza, Delsy Dávila-vera, Alirio Balza-quintero, Rosa Virginia Mendoza-briceño, Luisana AvilánAbstract: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 Kd 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.
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enolase as a plasminogen binding protein in Leishmania mexicana
Parasitology Research, 2007Co-Authors: Gilmer Vanegas, Wilfredo Quinones, Juan Luis Concepcion, Cesar Carrascolopez, Fernando Albericio, Luisana AvilánAbstract:Enolase is a glycolytic and gluconeogenic enzyme also found on the surface of several eukaryotic and prokaryotic cells where it acts as plasminogen binding protein. Leishmania mexicana, one of the causative agents of Leishmaniasis, binds plasminogen and, in this parasite, enolase has been previously found associated with the external face of the plasma membrane. In this work, we show that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plasminogen receptors. An internal motif 249AYDAERKMY257, similar to the nine amino-acid internal plasminogen-binding motif in Streptococcus pneumoniae enolase, is responsible for plasminogen interaction with the parasite enolase. Anti-enolase antibodies inhibited up to 60% of plasminogen binding on live parasites indicating that enolase act as a plasminogen receptor on the parasite. The fact that enolase acts as a possible plasminogen receptor in vivo makes this protein a promising target for therapy.
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Leishmania mexicana molecular cloning and characterization of enolase
Experimental Parasitology, 2007Co-Authors: Wilfredo Quinones, Ana J Caceres, Luisana Avilán, Priscila Pena, Maria Domingosananes, Paul A M Michels, Juan Luis ConcepcionAbstract:The gene of Leishmania mexicana enolase was cloned and overexpressed in Escherichia coli as an active enzyme; the protein was biochemically analyzed. This enolase shares with enolases from other trypanosomatids the presence of three atypical residues, each with a reactive side group, near the active site, already described for the enzyme from Trypanosoma brucei. The natural enzyme was purified, using a three-step procedure, from a cytosolic fraction of L. mexicana promastigotes. The kinetic properties of the purified recombinant enzyme were similar to those of the natural enzyme. Both the recombinant and natural enzyme were inhibited by inorganic pyrophosphate. Subcellular localization analysis after differential centrifugation showed that the enzyme activity is only associated with the cytosolic fraction. However, an apparently inactive form of enolase was detected by Western blots in the microsomal fraction. Digitonin treatment of parasites and immunofluorescence studies with permeabilized and non-permeabilized parasites showed that enolase is also associated with membranes and it was found at the external face of the plasma membrane.
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Purification and characterization of hexokinase from Leishmania mexicana
Parasitology Research, 2007Co-Authors: Miguel A. Pabón, Wilfredo Quinones, Ana J Caceres, Melisa Gualdrón, Luisana Avilán, Juan Luis ConcepcionAbstract:Hexokinase from Leishmania mexicana was purified to homogeneity from a glycosome-enriched fraction obtained after a differential centrifugation of promastigote form. The kinetic properties of the pure enzyme were determined and the Km values for glucose (Km = 66 μM) and ATP (Km = 303 μM) were comparable to those from hexokinase of Trypanosoma cruzi . L. mexicana hexokinase was able to use fructose (Km = 142 μM), which reflects the condition found in the insect host. In contrast with hexokinases from other trypanosomatids, the enzyme exhibited a moderate sensitivity to inhibition by glucose 6-phosphate. This inhibition was competitive with respect to both ATP and glucose, indicating that an allosteric site for glucose 6-phosphate does not exist in this enzyme. The enzyme was also inhibited by inorganic pyrophosphate, the inhibition being higher than that observed for T. cruzi enzyme. As expected, the enzyme was localized, by immunofluorescence analysis, in glycosomes and is present in both promastigotes and true amastigotes obtained from hamster lesion. Hexokinase specific activity increased with the aging of promastigote culture, and this increment was related to glucose consumption. However, the level of the hexokinase protein remains constant as determined by Western blotting. Several hypotheses are discussed to explain this result.
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Leishmania mexicana: Molecular cloning and characterization of enolase ☆
Experimental Parasitology, 2007Co-Authors: Wilfredo Quinones, Ana J Caceres, Luisana Avilán, Priscila Pena, Paul A M Michels, Maria Domingo-sananes, Juan Luis ConcepcionAbstract:The gene of Leishmania mexicana enolase was cloned and overexpressed in Escherichia coli as an active enzyme; the protein was biochemically analyzed. This enolase shares with enolases from other trypanosomatids the presence of three atypical residues, each with a reactive side group, near the active site, already described for the enzyme from Trypanosoma brucei. The natural enzyme was purified, using a three-step procedure, from a cytosolic fraction of L. mexicana promastigotes. The kinetic properties of the purified recombinant enzyme were similar to those of the natural enzyme. Both the recombinant and natural enzyme were inhibited by inorganic pyrophosphate. Subcellular localization analysis after differential centrifugation showed that the enzyme activity is only associated with the cytosolic fraction. However, an apparently inactive form of enolase was detected by Western blots in the microsomal fraction. Digitonin treatment of parasites and immunofluorescence studies with permeabilized and non-permeabilized parasites showed that enolase is also associated with membranes and it was found at the external face of the plasma membrane.
Graham H Coombs - One of the best experts on this subject based on the ideXlab platform.
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Subcellular localisation of purinemetabolising enzymes in Leishmania mexicana mexicana
Comparative Biochemistry and Physiology B, 2010Co-Authors: H.f. Hassan, J.c. Mottram, Graham H CoombsAbstract:Abstract 1. 1. Leishmania mexicana mexicana cultured promastigotes were fractionated by isopycnic centrifugation on linear sucrose gradients. 2. 2. Guanine, hypoxanthine and xanthine phosphoribosyltransferase activities were found to be associated with glycosomes, whereas adenine phosphoribosyltransferase was cytosolic. 3. 3. 3′- and 5′-nucleotidases and IMP dehydrogenase were shown to be particulate, the former two possibly being associated with the plasma membrane, IMP dehydrogenase with the endoplasmic reticulum. 4. 4. Nucleosidases and deaminases were found to be cytosolic. 5. 5. The results demonstrate that intracellular separation of enzymes could play a part in the regulation of the parasite's purine metabolism.
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Purine phosphoribosyltransferases of Leishmania mexicana mexicana and other flagellate protozoa.
Comparative Biochemistry and Physiology B, 2010Co-Authors: H.f. Hassan, Graham H CoombsAbstract:Abstract 1. 1. Amastigotes and cultured promastigotes of Leishmania mexicana mexicana and L. m. amazonensis , cultured promastigotes of L. donovani and L. tarentolae , and the culture forms of Crithidia fasciculata, Herpetomonas muscarum muscarum and H. m. ingenoplastis all possessed four phosphoribosyltransferase (PRTase) activities: adenine PRTase, hypoxanthine PRTase, guanine PRTase and xanthine PRTase. 2. 2. The enzymes of L. m. mexicana required divalent cations for activity; Mn 2+ or Co 2+ produced maximal activity in most cases. 3. 3. Hypoxanthine PRTase, guanine PRTase and xanthine PRTase from all organisms were sedimentable in part, suggesting that they may occur within glycosomes. 4. 4. The enzymes of L. m. mexicana cultured promastigotes were inhibited by a range of purine analogues.
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expression and characterization of a recombinant cysteine proteinase of Leishmania mexicana
Biochemical Journal, 2000Co-Authors: Sanya J Sanderson, Kevin G J Pollock, James D Hilley, Morten Meldal, Phaedria M St Hilaire, Maria A Juliano, Luiz Juliano, Jeremy C Mottram, Graham H CoombsAbstract:A major cysteine proteinase (CPB) of Leishmania mexicana, that is predominantly expressed in the form of the parasite that causes disease in mammals, has been overexpressed in Escherichia coli and purified from inclusion bodies to apparent homogeneity. The CPB enzyme, CPB2.8, was expressed as an inactive pro-form lacking the characteristic C-terminal extension (CPB2.8DeltaCTE). Pro-region processing was initiated during protein refolding and proceeded through several intermediate stages. Maximum enzyme activity accompanied removal of the entire pro-region. This was facilitated by acidification. Purified mature enzyme gave a single band on SDS/PAGE and gelatin SDS/PAGE gels, co-migrated with native enzyme in L. mexicana lysates, and had the same N-terminal sequence as the native enzyme. The procedure yielded >3.5 mg of active enzyme per litre of E. coli culture.
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Expression and characterization of a recombinant cysteine proteinase of Leishmania mexicana
Biochemical Journal, 2000Co-Authors: Sanya J Sanderson, Kevin G J Pollock, James D Hilley, Morten Meldal, Phaedria M St Hilaire, Maria A Juliano, Luiz Juliano, Jeremy C Mottram, Graham H CoombsAbstract:A major cysteine proteinase (CPB) of Leishmania mexicana, that is predominantly expressed in the form of the parasite that causes disease in mammals, has been overexpressed in Escherichia coli and purified from inclusion bodies to apparent homogeneity. The CPB enzyme, CPB2.8, was expressed as an inactive pro-form lacking the characteristic C-terminal extension (CPB2.8∆CTE). Pro-region processing was initiated during protein refolding and proceeded through several intermediate stages. Maximum enzyme activity accompanied removal of the entire pro-region. This was facilitated by acidification. Purified mature enzyme gave a single band on SDS/PAGE and gelatin SDS/PAGE gels, co-migrated with native enzyme in L. mexicana lysates, and had the same N-terminal sequence as the native enzyme. The procedure yielded > 3.5 mg of active enzyme per litre of E. coli culture.
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Expression of cysteine proteinases by metacyclic promastigotes of Leishmania mexicana.
Journal of Eukaryotic Microbiology, 1994Co-Authors: Paul A. Bates, Colin D. Robertson, Graham H CoombsAbstract:The expression of cysteine proteinases by metacyclic promastigotes of Leishmania mexicana was investigated using gelatin polyacrylamide gel electrophoresis. Two prominent bands were detected which distinguished metacyclics from multiplicative promastigotes, lacking detectable cysteine proteinase activity, and amastigotes, with a distinct banding pattern composed of multiple enzymes. A correlation between relative activity of the metacyclic-specific bands and the prevalence of metacyclics was found both during the growth cycle in vitro as metacyclogenesis occurred, and by comparison of stationary phase populations from consecutive subpassages in vitro. Irreversible inhibition of the metacyclic activities using N-benzyloxycarbonyl-phenylalanyl-alanyl diazomethane did not inhibit metacyclic to amastigote transformation in vitro. These activities provide a useful biochemical marker for the metacyclic promastigotes of L. mexicana.
Juan Luis Concepcion - One of the best experts on this subject based on the ideXlab platform.
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Plasminogen binding proteins in secreted membrane vesicles of Leishmania mexicana.
Molecular and Biochemical Parasitology, 2012Co-Authors: Lourdes Figuera, Wilfredo Quinones, Juan Luis Concepcion, Héctor Acosta, Amaranta Gómez-arreaza, Delsy Dávila-vera, Alirio Balza-quintero, Rosa Virginia Mendoza-briceño, Luisana AvilánAbstract: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 Kd 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.
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enolase as a plasminogen binding protein in Leishmania mexicana
Parasitology Research, 2007Co-Authors: Gilmer Vanegas, Wilfredo Quinones, Juan Luis Concepcion, Cesar Carrascolopez, Fernando Albericio, Luisana AvilánAbstract:Enolase is a glycolytic and gluconeogenic enzyme also found on the surface of several eukaryotic and prokaryotic cells where it acts as plasminogen binding protein. Leishmania mexicana, one of the causative agents of Leishmaniasis, binds plasminogen and, in this parasite, enolase has been previously found associated with the external face of the plasma membrane. In this work, we show that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plasminogen receptors. An internal motif 249AYDAERKMY257, similar to the nine amino-acid internal plasminogen-binding motif in Streptococcus pneumoniae enolase, is responsible for plasminogen interaction with the parasite enolase. Anti-enolase antibodies inhibited up to 60% of plasminogen binding on live parasites indicating that enolase act as a plasminogen receptor on the parasite. The fact that enolase acts as a possible plasminogen receptor in vivo makes this protein a promising target for therapy.
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Leishmania mexicana molecular cloning and characterization of enolase
Experimental Parasitology, 2007Co-Authors: Wilfredo Quinones, Ana J Caceres, Luisana Avilán, Priscila Pena, Maria Domingosananes, Paul A M Michels, Juan Luis ConcepcionAbstract:The gene of Leishmania mexicana enolase was cloned and overexpressed in Escherichia coli as an active enzyme; the protein was biochemically analyzed. This enolase shares with enolases from other trypanosomatids the presence of three atypical residues, each with a reactive side group, near the active site, already described for the enzyme from Trypanosoma brucei. The natural enzyme was purified, using a three-step procedure, from a cytosolic fraction of L. mexicana promastigotes. The kinetic properties of the purified recombinant enzyme were similar to those of the natural enzyme. Both the recombinant and natural enzyme were inhibited by inorganic pyrophosphate. Subcellular localization analysis after differential centrifugation showed that the enzyme activity is only associated with the cytosolic fraction. However, an apparently inactive form of enolase was detected by Western blots in the microsomal fraction. Digitonin treatment of parasites and immunofluorescence studies with permeabilized and non-permeabilized parasites showed that enolase is also associated with membranes and it was found at the external face of the plasma membrane.
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Purification and characterization of hexokinase from Leishmania mexicana
Parasitology Research, 2007Co-Authors: Miguel A. Pabón, Wilfredo Quinones, Ana J Caceres, Melisa Gualdrón, Luisana Avilán, Juan Luis ConcepcionAbstract:Hexokinase from Leishmania mexicana was purified to homogeneity from a glycosome-enriched fraction obtained after a differential centrifugation of promastigote form. The kinetic properties of the pure enzyme were determined and the Km values for glucose (Km = 66 μM) and ATP (Km = 303 μM) were comparable to those from hexokinase of Trypanosoma cruzi . L. mexicana hexokinase was able to use fructose (Km = 142 μM), which reflects the condition found in the insect host. In contrast with hexokinases from other trypanosomatids, the enzyme exhibited a moderate sensitivity to inhibition by glucose 6-phosphate. This inhibition was competitive with respect to both ATP and glucose, indicating that an allosteric site for glucose 6-phosphate does not exist in this enzyme. The enzyme was also inhibited by inorganic pyrophosphate, the inhibition being higher than that observed for T. cruzi enzyme. As expected, the enzyme was localized, by immunofluorescence analysis, in glycosomes and is present in both promastigotes and true amastigotes obtained from hamster lesion. Hexokinase specific activity increased with the aging of promastigote culture, and this increment was related to glucose consumption. However, the level of the hexokinase protein remains constant as determined by Western blotting. Several hypotheses are discussed to explain this result.
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Leishmania mexicana: Molecular cloning and characterization of enolase ☆
Experimental Parasitology, 2007Co-Authors: Wilfredo Quinones, Ana J Caceres, Luisana Avilán, Priscila Pena, Paul A M Michels, Maria Domingo-sananes, Juan Luis ConcepcionAbstract:The gene of Leishmania mexicana enolase was cloned and overexpressed in Escherichia coli as an active enzyme; the protein was biochemically analyzed. This enolase shares with enolases from other trypanosomatids the presence of three atypical residues, each with a reactive side group, near the active site, already described for the enzyme from Trypanosoma brucei. The natural enzyme was purified, using a three-step procedure, from a cytosolic fraction of L. mexicana promastigotes. The kinetic properties of the purified recombinant enzyme were similar to those of the natural enzyme. Both the recombinant and natural enzyme were inhibited by inorganic pyrophosphate. Subcellular localization analysis after differential centrifugation showed that the enzyme activity is only associated with the cytosolic fraction. However, an apparently inactive form of enolase was detected by Western blots in the microsomal fraction. Digitonin treatment of parasites and immunofluorescence studies with permeabilized and non-permeabilized parasites showed that enolase is also associated with membranes and it was found at the external face of the plasma membrane.
Wilfredo Quinones - One of the best experts on this subject based on the ideXlab platform.
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Plasminogen binding proteins in secreted membrane vesicles of Leishmania mexicana.
Molecular and Biochemical Parasitology, 2012Co-Authors: Lourdes Figuera, Wilfredo Quinones, Juan Luis Concepcion, Héctor Acosta, Amaranta Gómez-arreaza, Delsy Dávila-vera, Alirio Balza-quintero, Rosa Virginia Mendoza-briceño, Luisana AvilánAbstract: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 Kd 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.
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enolase as a plasminogen binding protein in Leishmania mexicana
Parasitology Research, 2007Co-Authors: Gilmer Vanegas, Wilfredo Quinones, Juan Luis Concepcion, Cesar Carrascolopez, Fernando Albericio, Luisana AvilánAbstract:Enolase is a glycolytic and gluconeogenic enzyme also found on the surface of several eukaryotic and prokaryotic cells where it acts as plasminogen binding protein. Leishmania mexicana, one of the causative agents of Leishmaniasis, binds plasminogen and, in this parasite, enolase has been previously found associated with the external face of the plasma membrane. In this work, we show that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plasminogen receptors. An internal motif 249AYDAERKMY257, similar to the nine amino-acid internal plasminogen-binding motif in Streptococcus pneumoniae enolase, is responsible for plasminogen interaction with the parasite enolase. Anti-enolase antibodies inhibited up to 60% of plasminogen binding on live parasites indicating that enolase act as a plasminogen receptor on the parasite. The fact that enolase acts as a possible plasminogen receptor in vivo makes this protein a promising target for therapy.
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Leishmania mexicana molecular cloning and characterization of enolase
Experimental Parasitology, 2007Co-Authors: Wilfredo Quinones, Ana J Caceres, Luisana Avilán, Priscila Pena, Maria Domingosananes, Paul A M Michels, Juan Luis ConcepcionAbstract:The gene of Leishmania mexicana enolase was cloned and overexpressed in Escherichia coli as an active enzyme; the protein was biochemically analyzed. This enolase shares with enolases from other trypanosomatids the presence of three atypical residues, each with a reactive side group, near the active site, already described for the enzyme from Trypanosoma brucei. The natural enzyme was purified, using a three-step procedure, from a cytosolic fraction of L. mexicana promastigotes. The kinetic properties of the purified recombinant enzyme were similar to those of the natural enzyme. Both the recombinant and natural enzyme were inhibited by inorganic pyrophosphate. Subcellular localization analysis after differential centrifugation showed that the enzyme activity is only associated with the cytosolic fraction. However, an apparently inactive form of enolase was detected by Western blots in the microsomal fraction. Digitonin treatment of parasites and immunofluorescence studies with permeabilized and non-permeabilized parasites showed that enolase is also associated with membranes and it was found at the external face of the plasma membrane.
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Purification and characterization of hexokinase from Leishmania mexicana
Parasitology Research, 2007Co-Authors: Miguel A. Pabón, Wilfredo Quinones, Ana J Caceres, Melisa Gualdrón, Luisana Avilán, Juan Luis ConcepcionAbstract:Hexokinase from Leishmania mexicana was purified to homogeneity from a glycosome-enriched fraction obtained after a differential centrifugation of promastigote form. The kinetic properties of the pure enzyme were determined and the Km values for glucose (Km = 66 μM) and ATP (Km = 303 μM) were comparable to those from hexokinase of Trypanosoma cruzi . L. mexicana hexokinase was able to use fructose (Km = 142 μM), which reflects the condition found in the insect host. In contrast with hexokinases from other trypanosomatids, the enzyme exhibited a moderate sensitivity to inhibition by glucose 6-phosphate. This inhibition was competitive with respect to both ATP and glucose, indicating that an allosteric site for glucose 6-phosphate does not exist in this enzyme. The enzyme was also inhibited by inorganic pyrophosphate, the inhibition being higher than that observed for T. cruzi enzyme. As expected, the enzyme was localized, by immunofluorescence analysis, in glycosomes and is present in both promastigotes and true amastigotes obtained from hamster lesion. Hexokinase specific activity increased with the aging of promastigote culture, and this increment was related to glucose consumption. However, the level of the hexokinase protein remains constant as determined by Western blotting. Several hypotheses are discussed to explain this result.
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Leishmania mexicana: Molecular cloning and characterization of enolase ☆
Experimental Parasitology, 2007Co-Authors: Wilfredo Quinones, Ana J Caceres, Luisana Avilán, Priscila Pena, Paul A M Michels, Maria Domingo-sananes, Juan Luis ConcepcionAbstract:The gene of Leishmania mexicana enolase was cloned and overexpressed in Escherichia coli as an active enzyme; the protein was biochemically analyzed. This enolase shares with enolases from other trypanosomatids the presence of three atypical residues, each with a reactive side group, near the active site, already described for the enzyme from Trypanosoma brucei. The natural enzyme was purified, using a three-step procedure, from a cytosolic fraction of L. mexicana promastigotes. The kinetic properties of the purified recombinant enzyme were similar to those of the natural enzyme. Both the recombinant and natural enzyme were inhibited by inorganic pyrophosphate. Subcellular localization analysis after differential centrifugation showed that the enzyme activity is only associated with the cytosolic fraction. However, an apparently inactive form of enolase was detected by Western blots in the microsomal fraction. Digitonin treatment of parasites and immunofluorescence studies with permeabilized and non-permeabilized parasites showed that enolase is also associated with membranes and it was found at the external face of the plasma membrane.
Gilmer Vanegas - One of the best experts on this subject based on the ideXlab platform.
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enolase as a plasminogen binding protein in Leishmania mexicana
Parasitology Research, 2007Co-Authors: Gilmer Vanegas, Wilfredo Quinones, Juan Luis Concepcion, Cesar Carrascolopez, Fernando Albericio, Luisana AvilánAbstract:Enolase is a glycolytic and gluconeogenic enzyme also found on the surface of several eukaryotic and prokaryotic cells where it acts as plasminogen binding protein. Leishmania mexicana, one of the causative agents of Leishmaniasis, binds plasminogen and, in this parasite, enolase has been previously found associated with the external face of the plasma membrane. In this work, we show that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plasminogen receptors. An internal motif 249AYDAERKMY257, similar to the nine amino-acid internal plasminogen-binding motif in Streptococcus pneumoniae enolase, is responsible for plasminogen interaction with the parasite enolase. Anti-enolase antibodies inhibited up to 60% of plasminogen binding on live parasites indicating that enolase act as a plasminogen receptor on the parasite. The fact that enolase acts as a possible plasminogen receptor in vivo makes this protein a promising target for therapy.