Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom

<p>Abstract</p> <p>Background</p> <p>Neutrophil migration to an inflamed site constitutes the first line of the innate immune response against invading microorganisms. Given the crucial role of endogenous lectins in neutrophil mobilization and activation, lectins from e...

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Main Authors: Fernandes Luiz, Fugii Gabriel M, Gimenez Ana, Schwartz Carolina, Tomazeli Luciane, Elifio-Esposito Selene, Zishler Luciana FM, Stuelp-Campelo Patrícia M, Moreno Andréa N
Format: Article
Language:English
Published: BMC 2011-01-01
Series:BMC Immunology
Online Access:http://www.biomedcentral.com/1471-2172/12/10
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spelling doaj-1854eb1e0d1c4177803a733ec4428cd72020-11-25T03:35:47ZengBMCBMC Immunology1471-21722011-01-011211010.1186/1471-2172-12-10Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venomFernandes LuizFugii Gabriel MGimenez AnaSchwartz CarolinaTomazeli LucianeElifio-Esposito SeleneZishler Luciana FMStuelp-Campelo Patrícia MMoreno Andréa N<p>Abstract</p> <p>Background</p> <p>Neutrophil migration to an inflamed site constitutes the first line of the innate immune response against invading microorganisms. Given the crucial role of endogenous lectins in neutrophil mobilization and activation, lectins from exogenous sources have often been considered as putative modulators of leukocyte function. Lectins purified from snake venom have been described as galactoside ligands that induce erythrocyte agglutination and platelet aggregation. This study evaluated human neutrophil migration and activation by C-type lectin BJcuL purified from <it>Bothrops jararacussu </it>venom.</p> <p>Results</p> <p>Utilizing fluorescence microscopy, we observed that biotinylated-BJcuL was evenly distributed on the neutrophil surface, selectively inhibited by D-galactose. Lectin was able to induce modification in the neutrophil morphology in a spherical shape for a polarized observed by optical microscopy and exposure to BJcuL in a Boyden chamber assay resulted in cell migration. After 30 minutes of incubation with BJcuL we found enhanced neutrophil functions, such as respiratory burst, zymozan phagocytosis and an increase in lissosomal volume. In addition, BJcuL delays late apoptosis neutrophils.</p> <p>Conclusion</p> <p>These results demonstrate that BJcuL can be implicated in a wide variety of immunological functions including first-line defense against pathogens, cell trafficking and induction of the innate immune response since lectin was capable of inducing potent neutrophil activation.</p> http://www.biomedcentral.com/1471-2172/12/10
collection DOAJ
language English
format Article
sources DOAJ
author Fernandes Luiz
Fugii Gabriel M
Gimenez Ana
Schwartz Carolina
Tomazeli Luciane
Elifio-Esposito Selene
Zishler Luciana FM
Stuelp-Campelo Patrícia M
Moreno Andréa N
spellingShingle Fernandes Luiz
Fugii Gabriel M
Gimenez Ana
Schwartz Carolina
Tomazeli Luciane
Elifio-Esposito Selene
Zishler Luciana FM
Stuelp-Campelo Patrícia M
Moreno Andréa N
Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom
BMC Immunology
author_facet Fernandes Luiz
Fugii Gabriel M
Gimenez Ana
Schwartz Carolina
Tomazeli Luciane
Elifio-Esposito Selene
Zishler Luciana FM
Stuelp-Campelo Patrícia M
Moreno Andréa N
author_sort Fernandes Luiz
title Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom
title_short Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom
title_full Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom
title_fullStr Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom
title_full_unstemmed Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from <it>Bothrops jararacussu </it>venom
title_sort human neutrophil migration and activation by bjcul, a galactose binding lectin purified from <it>bothrops jararacussu </it>venom
publisher BMC
series BMC Immunology
issn 1471-2172
publishDate 2011-01-01
description <p>Abstract</p> <p>Background</p> <p>Neutrophil migration to an inflamed site constitutes the first line of the innate immune response against invading microorganisms. Given the crucial role of endogenous lectins in neutrophil mobilization and activation, lectins from exogenous sources have often been considered as putative modulators of leukocyte function. Lectins purified from snake venom have been described as galactoside ligands that induce erythrocyte agglutination and platelet aggregation. This study evaluated human neutrophil migration and activation by C-type lectin BJcuL purified from <it>Bothrops jararacussu </it>venom.</p> <p>Results</p> <p>Utilizing fluorescence microscopy, we observed that biotinylated-BJcuL was evenly distributed on the neutrophil surface, selectively inhibited by D-galactose. Lectin was able to induce modification in the neutrophil morphology in a spherical shape for a polarized observed by optical microscopy and exposure to BJcuL in a Boyden chamber assay resulted in cell migration. After 30 minutes of incubation with BJcuL we found enhanced neutrophil functions, such as respiratory burst, zymozan phagocytosis and an increase in lissosomal volume. In addition, BJcuL delays late apoptosis neutrophils.</p> <p>Conclusion</p> <p>These results demonstrate that BJcuL can be implicated in a wide variety of immunological functions including first-line defense against pathogens, cell trafficking and induction of the innate immune response since lectin was capable of inducing potent neutrophil activation.</p>
url http://www.biomedcentral.com/1471-2172/12/10
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