Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and β-hematin
Identifieur interne : 000931 ( Istex/Corpus ); précédent : 000930; suivant : 000932Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and β-hematin
Auteurs : Mary M. Chen ; Lirong Shi ; David J. Sullivan Jr.Source :
- Molecular & Biochemical Parasitology [ 0166-6851 ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Antimalarial, Chloroquine, Columbae, Columbae heme polymers, Degradation, Erythrocyte, Falciparum, Falciparum heme polymer, Feisem, Haemoproteus, Heme, Heme monomer, Heme pigments, Heme polymer, Heme polymer extension, Heme polymer formation, Heme polymers, Hemozoin, Mansoni, Monomer, Parasite, Parasitology, Plasmodium, Polymer, Quinoline, Quinoline inhibition, Quinolines, Schistosoma, Schistosoma mansoni.
Abstract
Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.
Url:
DOI: 10.1016/S0166-6851(00)00365-0
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.</div>
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<abstract>Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.</abstract>
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<note type="content">Fig. 1: Pigment in H. columbae gametocytes. A thin blood film of nucleated erythrocytes from the Rock dove pigeon, Columbia livia, infected with H. columbae gametocytes was photographed at 1000× magnification. Approximately 20 black pigment granules are visible diffusely within a gametocyte.</note>
<note type="content">Fig. 2: FTIR spectra of heme polymers from P. falciparum (a), β-hematin (b), S. mansoni (c), and H. columbae (d) show the signature peaks for the heme polymer at 1207 and 1660 cm−1 from stretching of the carbon–oxygen bond of the proprionate carbonyl group by iron.</note>
<note type="content">Fig. 3: FEISEM of heme polymer purified from parasites. P. falciparum (a), β-hematin (b), S. mansoni (c), and H. columbae (d) heme polymers have distinct three-dimensional shapes and sizes, as seen at approximately 100 000×.</note>
<note type="content">Fig. 4: (A) Inhibition of heme polymer extension by the quinolines. Control incubations of heme (H) alone and heme polymer (HP) alone were purified alongside incubations of H+HP without and with quinoline drugs. All parasite heme polymers function as a template for heme polymer extension by heme monomer that is inhibitable by chloroquine (CQ), amodiaquine (AQ) and quinidine (QD). P. falciparum (filled bars), β-hematin (empty bars), S. mansoni (dotted bars), and H. columbae (slanted bars) values for purified heme polymer are S.E.M. of triplicate samples. (B) Inhibition of heme polymer extension by increasing concentrations of chloroquine. P. falciparum (filled squares, HZ), β-hematin (empty squares, β-H) heme polymer templates had lower concentrations of chloroquine that inhibited half of new polymer extension than S. mansoni (filled triangles, S), and H. columbae (empty triangles, HPr). Lines are best fit with no difference in rate of decrease for all heme polymers but with a statistically significant higher y axis value for P. falciparum and β-hematin as compared to S. mansoni and H. columbae (P<0.00001).</note>
<note type="content">Fig. 5: FEISEM of heme polymer extension assay products. Test tube extension of P. falciparum (a), β-hematin (b), S. mansoni (c), and H. columbae (d) heme polymer depicted a spiculated addition that did not resemble original template as seen with FEISEM in Fig. 3.</note>
<note type="content">Fig. 6: Degradation of heme polymers by H2O2. Heme polymer content of trophozoite lysates and the purified pigments were equalized to 10 nmol before incubations in an acid pH overnight with H2O2 in concentrations ranging from 5 to 100 mM. The concentration of H2O2 degrading half of the heme polymers is summarized as a single value. 2 mM H2O2 completely degrades heme monomer in 1–2 h. Results are S.E.M. of triplicate samples repeated on at least two separate days.</note>
<note type="content">Fig. 7: FEISEM of heme polymer degradation by H2O2 at a pH of 5.0. The morphology shows pitting with P. falciparum (a), decrease in size with spicule formation with β-hematin (b), decrease in size with S. mansoni (c), and more pitting with H. columbae (d).</note>
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<note type="correspondence"><p>Corresponding author. Tel: +1-410-6141562; fax: +1-410-9550105</p>
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<abstract xml:lang="en"><p>Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.</p>
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<textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head>
<item><term>Hemozoin</term>
</item>
<item><term>Heme polymer</term>
</item>
<item><term>Quinoline</term>
</item>
<item><term>Plasmodium falciparum</term>
</item>
<item><term>Schistosoma mansoni</term>
</item>
<item><term>Haemoproteus columbae</term>
</item>
</list>
</keywords>
</textClass>
<textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head>
<item><term>FEISEM, field emission inlens scanning electron microscopy</term>
</item>
<item><term>FTIR=Fourier-transform infrared</term>
</item>
<item><term>H2O2, hydrogen peroxide</term>
</item>
<item><term>SDS, sodium dodecyl sulfate</term>
</item>
</list>
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<head><ce:title><ce:italic>Haemoproteus</ce:italic>
and <ce:italic>Schistosoma</ce:italic>
synthesize heme polymers similar to <ce:italic>Plasmodium</ce:italic>
hemozoin and β-hematin</ce:title>
<ce:author-group><ce:author><ce:given-name>Mary M.</ce:given-name>
<ce:surname>Chen</ce:surname>
</ce:author>
<ce:author><ce:given-name>Lirong</ce:given-name>
<ce:surname>Shi</ce:surname>
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<ce:author><ce:given-name>David J.</ce:given-name>
<ce:surname>Sullivan</ce:surname>
<ce:suffix>Jr.</ce:suffix>
<ce:cross-ref refid="CORR1">*</ce:cross-ref>
<ce:e-address>dsulliva@jhsph.edu</ce:e-address>
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<ce:affiliation><ce:textfn>The W. Harry Feinstone Department of Molecular Microbiology and Immunology, School of Hygiene and Public Health, Room 5005 Hygiene Boulevard, Johns Hopkins University, 615 North Wolfe Street, Baltimore, MD, 21205 USA</ce:textfn>
</ce:affiliation>
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<ce:text>Corresponding author. Tel: +1-410-6141562; fax: +1-410-9550105</ce:text>
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<ce:abstract><ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec><ce:simple-para>Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by <ce:italic>Haemoproteus columbae</ce:italic>
and <ce:italic>Schistosoma mansoni</ce:italic>
to that of <ce:italic>Plasmodium</ce:italic>
<ce:italic>falciparum</ce:italic>
hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both <ce:italic>P. falciparum</ce:italic>
and <ce:italic>H. columbae</ce:italic>
heme polymers had a symmetrical shape unlike the amorphous <ce:italic>S. mansoni</ce:italic>
heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, <ce:italic>Haemoproteus</ce:italic>
, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
<ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title>
<ce:keyword><ce:text>Hemozoin</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Heme polymer</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Quinoline</ce:text>
</ce:keyword>
<ce:keyword><ce:text><ce:italic>Plasmodium falciparum</ce:italic>
</ce:text>
</ce:keyword>
<ce:keyword><ce:text><ce:italic>Schistosoma mansoni</ce:italic>
</ce:text>
</ce:keyword>
<ce:keyword><ce:text><ce:italic>Haemoproteus columbae</ce:italic>
</ce:text>
</ce:keyword>
</ce:keywords>
<ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title>
<ce:keyword><ce:text>FEISEM, field emission inlens scanning electron microscopy</ce:text>
</ce:keyword>
<ce:keyword><ce:text>FTIR=Fourier-transform infrared</ce:text>
</ce:keyword>
<ce:keyword><ce:text>H<ce:inf>2</ce:inf>
O<ce:inf>2</ce:inf>
, hydrogen peroxide</ce:text>
</ce:keyword>
<ce:keyword><ce:text>SDS, sodium dodecyl sulfate</ce:text>
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<abstract lang="en">Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.</abstract>
<note type="content">Fig. 1: Pigment in H. columbae gametocytes. A thin blood film of nucleated erythrocytes from the Rock dove pigeon, Columbia livia, infected with H. columbae gametocytes was photographed at 1000× magnification. Approximately 20 black pigment granules are visible diffusely within a gametocyte.</note>
<note type="content">Fig. 2: FTIR spectra of heme polymers from P. falciparum (a), β-hematin (b), S. mansoni (c), and H. columbae (d) show the signature peaks for the heme polymer at 1207 and 1660 cm−1 from stretching of the carbon–oxygen bond of the proprionate carbonyl group by iron.</note>
<note type="content">Fig. 3: FEISEM of heme polymer purified from parasites. P. falciparum (a), β-hematin (b), S. mansoni (c), and H. columbae (d) heme polymers have distinct three-dimensional shapes and sizes, as seen at approximately 100 000×.</note>
<note type="content">Fig. 4: (A) Inhibition of heme polymer extension by the quinolines. Control incubations of heme (H) alone and heme polymer (HP) alone were purified alongside incubations of H+HP without and with quinoline drugs. All parasite heme polymers function as a template for heme polymer extension by heme monomer that is inhibitable by chloroquine (CQ), amodiaquine (AQ) and quinidine (QD). P. falciparum (filled bars), β-hematin (empty bars), S. mansoni (dotted bars), and H. columbae (slanted bars) values for purified heme polymer are S.E.M. of triplicate samples. (B) Inhibition of heme polymer extension by increasing concentrations of chloroquine. P. falciparum (filled squares, HZ), β-hematin (empty squares, β-H) heme polymer templates had lower concentrations of chloroquine that inhibited half of new polymer extension than S. mansoni (filled triangles, S), and H. columbae (empty triangles, HPr). Lines are best fit with no difference in rate of decrease for all heme polymers but with a statistically significant higher y axis value for P. falciparum and β-hematin as compared to S. mansoni and H. columbae (P<0.00001).</note>
<note type="content">Fig. 5: FEISEM of heme polymer extension assay products. Test tube extension of P. falciparum (a), β-hematin (b), S. mansoni (c), and H. columbae (d) heme polymer depicted a spiculated addition that did not resemble original template as seen with FEISEM in Fig. 3.</note>
<note type="content">Fig. 6: Degradation of heme polymers by H2O2. Heme polymer content of trophozoite lysates and the purified pigments were equalized to 10 nmol before incubations in an acid pH overnight with H2O2 in concentrations ranging from 5 to 100 mM. The concentration of H2O2 degrading half of the heme polymers is summarized as a single value. 2 mM H2O2 completely degrades heme monomer in 1–2 h. Results are S.E.M. of triplicate samples repeated on at least two separate days.</note>
<note type="content">Fig. 7: FEISEM of heme polymer degradation by H2O2 at a pH of 5.0. The morphology shows pitting with P. falciparum (a), decrease in size with spicule formation with β-hematin (b), decrease in size with S. mansoni (c), and more pitting with H. columbae (d).</note>
<subject lang="en"><genre>Keywords</genre>
<topic>Hemozoin</topic>
<topic>Heme polymer</topic>
<topic>Quinoline</topic>
<topic>Plasmodium falciparum</topic>
<topic>Schistosoma mansoni</topic>
<topic>Haemoproteus columbae</topic>
</subject>
<subject lang="en"><genre>Abbreviations</genre>
<topic>FEISEM, field emission inlens scanning electron microscopy</topic>
<topic>FTIR=Fourier-transform infrared</topic>
<topic>H2O2, hydrogen peroxide</topic>
<topic>SDS, sodium dodecyl sulfate</topic>
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