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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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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