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Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae

Salivary gland homogenate (SGH) from the female mosquitoes Anopheles gambiae, An. stephensi, An. freeborni, An. dirus and An. albimanus were found to exhibit hemagglutinating (lectin) activity. Lectin activity was not found for male An. gambiae, or female Ae aegypti, Culex quinquefasciatus, Phleboto...

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Autores principales: Francischetti, Ivo M. B., Ma, Dongying, Andersen, John F., Ribeiro, José M. C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4160252/
https://www.ncbi.nlm.nih.gov/pubmed/25207644
http://dx.doi.org/10.1371/journal.pone.0107295
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author Francischetti, Ivo M. B.
Ma, Dongying
Andersen, John F.
Ribeiro, José M. C.
author_facet Francischetti, Ivo M. B.
Ma, Dongying
Andersen, John F.
Ribeiro, José M. C.
author_sort Francischetti, Ivo M. B.
collection PubMed
description Salivary gland homogenate (SGH) from the female mosquitoes Anopheles gambiae, An. stephensi, An. freeborni, An. dirus and An. albimanus were found to exhibit hemagglutinating (lectin) activity. Lectin activity was not found for male An. gambiae, or female Ae aegypti, Culex quinquefasciatus, Phlebotomus duboscqi, and Lutzomyia longipalpis. With respect to species-specificity, An. gambiae SGH agglutinates red blood cells (RBC) from humans, horse, sheep, goat, pig, and cow; it is less active for rats RBC, and not detectable for guinea-pigs or chicken RBC. Notably, lectin activity was inhibited by low concentrations of dextran sulfate 50–500 K, fucoidan, heparin, laminin, heparin sulfate proteoglycan, sialyl-containing glycans (e.g. 3′-sialyl Lewis X, and 6′-sialyl lactose), and gangliosides (e.g. GM3, GD1, GD1b, GTB1, GM1, GQ1B), but not by simple sugars. These results imply that molecule(s) in the salivary gland target sulfated glycans. SGH from An. gambiae was also found to promote agglutination of HL-60 cells which are rich in sialyl Lewis X, a glycan that decorates PSGL-1, the neutrophils receptor that interacts with endothelial cell P-selectin. Accordingly, SGH interferes with HL-60 cells adhesion to immobilized P-selectin. Because An. gambiae SGH expresses galectins, one member of this family (herein named Agalectin) was expressed in E. coli. Recombinant Agalectin behaves as a non-covalent homodimer. It does not display lectin activity, and does not interact with 500 candidates tested in a Glycan microarray. Gel-filtration chromatography of the SGH of An. gambiae identified a fraction with hemagglutinating activity, which was analyzed by 1D PAGE followed by in-gel tryptic digestion, and nano-LC MS/MS. This approach identified several genes which emerge as candidates for a lectin targeting sulfated glycans, the first with this selectivity to be reported in the SGH of a blood-sucking arthropod. The role of salivary molecules (sialogenins) with lectin activity is discussed in the context of inflammation, and parasite-vector-host interactions.
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spelling pubmed-41602522014-09-12 Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae Francischetti, Ivo M. B. Ma, Dongying Andersen, John F. Ribeiro, José M. C. PLoS One Research Article Salivary gland homogenate (SGH) from the female mosquitoes Anopheles gambiae, An. stephensi, An. freeborni, An. dirus and An. albimanus were found to exhibit hemagglutinating (lectin) activity. Lectin activity was not found for male An. gambiae, or female Ae aegypti, Culex quinquefasciatus, Phlebotomus duboscqi, and Lutzomyia longipalpis. With respect to species-specificity, An. gambiae SGH agglutinates red blood cells (RBC) from humans, horse, sheep, goat, pig, and cow; it is less active for rats RBC, and not detectable for guinea-pigs or chicken RBC. Notably, lectin activity was inhibited by low concentrations of dextran sulfate 50–500 K, fucoidan, heparin, laminin, heparin sulfate proteoglycan, sialyl-containing glycans (e.g. 3′-sialyl Lewis X, and 6′-sialyl lactose), and gangliosides (e.g. GM3, GD1, GD1b, GTB1, GM1, GQ1B), but not by simple sugars. These results imply that molecule(s) in the salivary gland target sulfated glycans. SGH from An. gambiae was also found to promote agglutination of HL-60 cells which are rich in sialyl Lewis X, a glycan that decorates PSGL-1, the neutrophils receptor that interacts with endothelial cell P-selectin. Accordingly, SGH interferes with HL-60 cells adhesion to immobilized P-selectin. Because An. gambiae SGH expresses galectins, one member of this family (herein named Agalectin) was expressed in E. coli. Recombinant Agalectin behaves as a non-covalent homodimer. It does not display lectin activity, and does not interact with 500 candidates tested in a Glycan microarray. Gel-filtration chromatography of the SGH of An. gambiae identified a fraction with hemagglutinating activity, which was analyzed by 1D PAGE followed by in-gel tryptic digestion, and nano-LC MS/MS. This approach identified several genes which emerge as candidates for a lectin targeting sulfated glycans, the first with this selectivity to be reported in the SGH of a blood-sucking arthropod. The role of salivary molecules (sialogenins) with lectin activity is discussed in the context of inflammation, and parasite-vector-host interactions. Public Library of Science 2014-09-10 /pmc/articles/PMC4160252/ /pubmed/25207644 http://dx.doi.org/10.1371/journal.pone.0107295 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.
spellingShingle Research Article
Francischetti, Ivo M. B.
Ma, Dongying
Andersen, John F.
Ribeiro, José M. C.
Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae
title Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae
title_full Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae
title_fullStr Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae
title_full_unstemmed Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae
title_short Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae
title_sort evidence for a lectin specific for sulfated glycans in the salivary gland of the malaria vector, anopheles gambiae
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4160252/
https://www.ncbi.nlm.nih.gov/pubmed/25207644
http://dx.doi.org/10.1371/journal.pone.0107295
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