Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.

<h4>Background</h4>Hematophagous insects digest large amounts of host hemoglobin and release heme inside their guts. In Rhodnius prolixus, hemoglobin-derived heme is detoxified by biomineralization, forming hemozoin (Hz). Recently, the involvement of the R. prolixus perimicrovillar membr...

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Autores principales:	Flávia Borges Mury, José Roberto da Silva, Ligia Souza Ferreira, Beatriz dos Santos Ferreira, Gonçalo Apolinário de Souza-Filho, Jayme Augusto de Souza-Neto, Paulo Eduardo Martins Ribolla, Carlos Peres Silva, Viviane Veiga do Nascimento, Olga Lima Tavares Machado, Marília Amorim Berbert-Molina, Marilvia Dansa-Petretski
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5072708f7e9b45d490bcbf14ab42476e
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spelling	oai:doaj.org-article:5072708f7e9b45d490bcbf14ab42476e2021-11-25T06:20:30ZAlpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.1932-620310.1371/journal.pone.0006966https://doaj.org/article/5072708f7e9b45d490bcbf14ab42476e2009-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19742319/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Hematophagous insects digest large amounts of host hemoglobin and release heme inside their guts. In Rhodnius prolixus, hemoglobin-derived heme is detoxified by biomineralization, forming hemozoin (Hz). Recently, the involvement of the R. prolixus perimicrovillar membranes in Hz formation was demonstrated.<h4>Methodology/principal findings</h4>Hz formation activity of an alpha-glucosidase was investigated. Hz formation was inhibited by specific alpha-glucosidase inhibitors. Moreover, Hz formation was sensitive to inhibition by Diethypyrocarbonate, suggesting a critical role of histidine residues in enzyme activity. Additionally, a polyclonal antibody raised against a phytophagous insect alpha-glucosidase was able to inhibit Hz formation. The alpha-glucosidase inhibitors have had no effects when used 10 h after the start of reaction, suggesting that alpha-glucosidase should act in the nucleation step of Hz formation. Hz formation was seen to be dependent on the substrate-binding site of enzyme, in a way that maltose, an enzyme substrate, blocks such activity. dsRNA, constructed using the sequence of alpha-glucosidase gene, was injected into R. prolixus females' hemocoel. Gene silencing was accomplished by reduction of both alpha-glucosidase and Hz formation activities. Insects were fed on plasma or hemin-enriched plasma and gene expression and activity of alpha-glucosidase were higher in the plasma plus hemin-fed insects. The deduced amino acid sequence of alpha-glucosidase shows a high similarity to the insect alpha-glucosidases, with critical histidine and aspartic residues conserved among the enzymes.<h4>Conclusions/significance</h4>Herein the Hz formation is shown to be associated to an alpha-glucosidase, the biochemical marker from Hemipteran perimicrovillar membranes. Usually, these enzymes catalyze the hydrolysis of glycosidic bond. The results strongly suggest that alpha-glucosidase is responsible for Hz nucleation in the R. prolixus midgut, indicating that the plasticity of this enzyme may play an important role in conferring fitness to hemipteran hematophagy, for instance.Flávia Borges MuryJosé Roberto da SilvaLigia Souza FerreiraBeatriz dos Santos FerreiraGonçalo Apolinário de Souza-FilhoJayme Augusto de Souza-NetoPaulo Eduardo Martins RibollaCarlos Peres SilvaViviane Veiga do NascimentoOlga Lima Tavares MachadoMarília Amorim Berbert-MolinaMarilvia Dansa-PetretskiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 9, p e6966 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Flávia Borges Mury José Roberto da Silva Ligia Souza Ferreira Beatriz dos Santos Ferreira Gonçalo Apolinário de Souza-Filho Jayme Augusto de Souza-Neto Paulo Eduardo Martins Ribolla Carlos Peres Silva Viviane Veiga do Nascimento Olga Lima Tavares Machado Marília Amorim Berbert-Molina Marilvia Dansa-Petretski Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
description	<h4>Background</h4>Hematophagous insects digest large amounts of host hemoglobin and release heme inside their guts. In Rhodnius prolixus, hemoglobin-derived heme is detoxified by biomineralization, forming hemozoin (Hz). Recently, the involvement of the R. prolixus perimicrovillar membranes in Hz formation was demonstrated.<h4>Methodology/principal findings</h4>Hz formation activity of an alpha-glucosidase was investigated. Hz formation was inhibited by specific alpha-glucosidase inhibitors. Moreover, Hz formation was sensitive to inhibition by Diethypyrocarbonate, suggesting a critical role of histidine residues in enzyme activity. Additionally, a polyclonal antibody raised against a phytophagous insect alpha-glucosidase was able to inhibit Hz formation. The alpha-glucosidase inhibitors have had no effects when used 10 h after the start of reaction, suggesting that alpha-glucosidase should act in the nucleation step of Hz formation. Hz formation was seen to be dependent on the substrate-binding site of enzyme, in a way that maltose, an enzyme substrate, blocks such activity. dsRNA, constructed using the sequence of alpha-glucosidase gene, was injected into R. prolixus females' hemocoel. Gene silencing was accomplished by reduction of both alpha-glucosidase and Hz formation activities. Insects were fed on plasma or hemin-enriched plasma and gene expression and activity of alpha-glucosidase were higher in the plasma plus hemin-fed insects. The deduced amino acid sequence of alpha-glucosidase shows a high similarity to the insect alpha-glucosidases, with critical histidine and aspartic residues conserved among the enzymes.<h4>Conclusions/significance</h4>Herein the Hz formation is shown to be associated to an alpha-glucosidase, the biochemical marker from Hemipteran perimicrovillar membranes. Usually, these enzymes catalyze the hydrolysis of glycosidic bond. The results strongly suggest that alpha-glucosidase is responsible for Hz nucleation in the R. prolixus midgut, indicating that the plasticity of this enzyme may play an important role in conferring fitness to hemipteran hematophagy, for instance.
format	article
author	Flávia Borges Mury José Roberto da Silva Ligia Souza Ferreira Beatriz dos Santos Ferreira Gonçalo Apolinário de Souza-Filho Jayme Augusto de Souza-Neto Paulo Eduardo Martins Ribolla Carlos Peres Silva Viviane Veiga do Nascimento Olga Lima Tavares Machado Marília Amorim Berbert-Molina Marilvia Dansa-Petretski
author_facet	Flávia Borges Mury José Roberto da Silva Ligia Souza Ferreira Beatriz dos Santos Ferreira Gonçalo Apolinário de Souza-Filho Jayme Augusto de Souza-Neto Paulo Eduardo Martins Ribolla Carlos Peres Silva Viviane Veiga do Nascimento Olga Lima Tavares Machado Marília Amorim Berbert-Molina Marilvia Dansa-Petretski
author_sort	Flávia Borges Mury
title	Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
title_short	Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
title_full	Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
title_fullStr	Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
title_full_unstemmed	Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
title_sort	alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/5072708f7e9b45d490bcbf14ab42476e
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Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: an evolutionary history.

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