Purification and molecular characterization of a novel mannose-specific lectin from Dioclea reflexa hook seeds with inflammatory activity

A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G‐50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α‐methyl‐d‐mannoside, d‐mannose, and d...

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Veröffentlicht in:Journal of molecular recognition 2016-04, Vol.29 (4), p.134-141
Hauptverfasser: Pinto-Junior, Vanir R., Correia, Jorge L. A., Pereira, Ronniery I., Pereira-Junior, Francisco N., Santiago, Mayara Q., Osterne, Vinicius J. S., Madeira, Juliana C., Cajazeiras, João B., Nagano, Celso S., Delatorre, Plinio, Assreuy, Ana M. S., Nascimento, Kyria S., Cavada, Benildo S.
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container_end_page 141
container_issue 4
container_start_page 134
container_title Journal of molecular recognition
container_volume 29
creator Pinto-Junior, Vanir R.
Correia, Jorge L. A.
Pereira, Ronniery I.
Pereira-Junior, Francisco N.
Santiago, Mayara Q.
Osterne, Vinicius J. S.
Madeira, Juliana C.
Cajazeiras, João B.
Nagano, Celso S.
Delatorre, Plinio
Assreuy, Ana M. S.
Nascimento, Kyria S.
Cavada, Benildo S.
description A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G‐50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α‐methyl‐d‐mannoside, d‐mannose, and d‐glucose. The hemagglutinating activity of DrfL is optimum at pH 5.0–7.0, stable up to 50 °C, and dependent on divalent cations. Similar to other lectins of the subtribe Diocleinae, the analysis by mass spectrometry indicated that DrfL has three chains (α, β, and γ) with masses of 25 562, 12 874, and 12 706 Da, respectively, with no disulfide bonds or glycosylation. DrfL showed inflammatory activity in the paw edema model and exhibited low cytotoxicity against Artemia sp. Copyright © 2015 John Wiley & Sons, Ltd. A new mannose‐specific lectin from Dioclea reflexa Hook seeds (DrfL) was purified and partially characterized. DrfL toxic effect was evaluated against Artemia sp. DrfL elicits acute inflammation via lectin domain mediated by nitric oxide.
doi_str_mv 10.1002/jmr.2512
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The hemagglutinating activity of DrfL is optimum at pH 5.0–7.0, stable up to 50 °C, and dependent on divalent cations. Similar to other lectins of the subtribe Diocleinae, the analysis by mass spectrometry indicated that DrfL has three chains (α, β, and γ) with masses of 25 562, 12 874, and 12 706 Da, respectively, with no disulfide bonds or glycosylation. DrfL showed inflammatory activity in the paw edema model and exhibited low cytotoxicity against Artemia sp. Copyright © 2015 John Wiley &amp; Sons, Ltd. A new mannose‐specific lectin from Dioclea reflexa Hook seeds (DrfL) was purified and partially characterized. DrfL toxic effect was evaluated against Artemia sp. 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A.</creatorcontrib><creatorcontrib>Pereira, Ronniery I.</creatorcontrib><creatorcontrib>Pereira-Junior, Francisco N.</creatorcontrib><creatorcontrib>Santiago, Mayara Q.</creatorcontrib><creatorcontrib>Osterne, Vinicius J. S.</creatorcontrib><creatorcontrib>Madeira, Juliana C.</creatorcontrib><creatorcontrib>Cajazeiras, João B.</creatorcontrib><creatorcontrib>Nagano, Celso S.</creatorcontrib><creatorcontrib>Delatorre, Plinio</creatorcontrib><creatorcontrib>Assreuy, Ana M. S.</creatorcontrib><creatorcontrib>Nascimento, Kyria S.</creatorcontrib><creatorcontrib>Cavada, Benildo S.</creatorcontrib><title>Purification and molecular characterization of a novel mannose-specific lectin from Dioclea reflexa hook seeds with inflammatory activity</title><title>Journal of molecular recognition</title><addtitle>J. Mol. Recognit</addtitle><description>A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G‐50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α‐methyl‐d‐mannoside, d‐mannose, and d‐glucose. The hemagglutinating activity of DrfL is optimum at pH 5.0–7.0, stable up to 50 °C, and dependent on divalent cations. Similar to other lectins of the subtribe Diocleinae, the analysis by mass spectrometry indicated that DrfL has three chains (α, β, and γ) with masses of 25 562, 12 874, and 12 706 Da, respectively, with no disulfide bonds or glycosylation. DrfL showed inflammatory activity in the paw edema model and exhibited low cytotoxicity against Artemia sp. Copyright © 2015 John Wiley &amp; Sons, Ltd. A new mannose‐specific lectin from Dioclea reflexa Hook seeds (DrfL) was purified and partially characterized. DrfL toxic effect was evaluated against Artemia sp. 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A.</au><au>Pereira, Ronniery I.</au><au>Pereira-Junior, Francisco N.</au><au>Santiago, Mayara Q.</au><au>Osterne, Vinicius J. S.</au><au>Madeira, Juliana C.</au><au>Cajazeiras, João B.</au><au>Nagano, Celso S.</au><au>Delatorre, Plinio</au><au>Assreuy, Ana M. S.</au><au>Nascimento, Kyria S.</au><au>Cavada, Benildo S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and molecular characterization of a novel mannose-specific lectin from Dioclea reflexa hook seeds with inflammatory activity</atitle><jtitle>Journal of molecular recognition</jtitle><addtitle>J. Mol. Recognit</addtitle><date>2016-04</date><risdate>2016</risdate><volume>29</volume><issue>4</issue><spage>134</spage><epage>141</epage><pages>134-141</pages><issn>0952-3499</issn><eissn>1099-1352</eissn><abstract>A novel lectin present in Dioclea reflexa seeds (DrfL) was discovered and described in this study. DrfL was purified in a single step by affinity chromatography in a Sephadex G‐50 column. The lectin strongly agglutinated rabbit erythrocytes and was inhibited by α‐methyl‐d‐mannoside, d‐mannose, and d‐glucose. The hemagglutinating activity of DrfL is optimum at pH 5.0–7.0, stable up to 50 °C, and dependent on divalent cations. Similar to other lectins of the subtribe Diocleinae, the analysis by mass spectrometry indicated that DrfL has three chains (α, β, and γ) with masses of 25 562, 12 874, and 12 706 Da, respectively, with no disulfide bonds or glycosylation. DrfL showed inflammatory activity in the paw edema model and exhibited low cytotoxicity against Artemia sp. Copyright © 2015 John Wiley &amp; Sons, Ltd. A new mannose‐specific lectin from Dioclea reflexa Hook seeds (DrfL) was purified and partially characterized. DrfL toxic effect was evaluated against Artemia sp. DrfL elicits acute inflammation via lectin domain mediated by nitric oxide.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>26464029</pmid><doi>10.1002/jmr.2512</doi><tpages>8</tpages></addata></record>
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subjects Animals
Artemia
Chromatography, Affinity
Dioclea - chemistry
Dioclea reflexa
Edema
Edema - chemically induced
Erythrocytes
Erythrocytes - drug effects
ESI mass spectrometry
Hemagglutination - drug effects
Hooks
Inflammation Mediators - isolation & purification
Inflammation Mediators - pharmacology
inflammatory activity
lectin
Lectins
Mannose - pharmacology
Mice
Plant Lectins - chemistry
Plant Lectins - isolation & purification
Plant Lectins - pharmacology
Protein Structure, Secondary
Rabbits
Recognition
Seeds
Toxic
title Purification and molecular characterization of a novel mannose-specific lectin from Dioclea reflexa hook seeds with inflammatory activity
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