Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa

Detalhes bibliográficos
Autor(a) principal: Olivo-Díaz , Angélica
Data de Publicação: 2020
Outros Autores: Martínez-Ocaña, Joel, Maravilla, Pablo
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Revista do Instituto de Medicina Tropical de São Paulo
Texto Completo: https://www.revistas.usp.br/rimtsp/article/view/175931
Resumo: Intestinal mucins are the first line of defense against microorganisms. Although knowledge about the mechanisms involved in the establishment of intestinal protozoa is limited, there is evidence that these parasites produce lectin-like molecules and glycosidases, that exert both, constitutive and secretory functions, promoting the establishment of these microorganisms. In the present review, we analyse the main interactions between mucins of the host intestine and the four main protozoan parasites in humans and their implications in intestinal colonization. There are lectin-like molecules that contain complex oligosaccharide structures and N-acetylglucosamine (GlcNAc), mannose and sialic acid as main components, which are excreted/secreted by Giardia intestinalis, and recognized by the host using mannose-binding lectins (MBL). Entamoeba histolytica and Cryptosporidium spp. express the lectin galactose/N-acetyl-D-galactosamine, which facilitates their adhesion to cells. In Cryptosporidium, the glycoproteins gp30, gp40/15 and gp900 and the glycoprotein lectin CpClec are involved in protozoan adhesion to intestinal cells, forming an adhesion-attack complex. G. intestinalis and E. histolytica can also produce glycosidases such as β-N-acetyl-D-glucosaminidase, α-d-glucosidase, β-d-galactosidase, β-l-fucosidase, α-N-acetyl-d-galactosaminidase and β-mannosidase. In Blastocystis, α-D-mannose, α-D-glucose, GlcNAc, α-D-fucose, chitin and sialic acid that have been identified on their surface. Fucosidases, hexosaminidases and polygalacturonases, which may be involved in the mucin degradation process, have also been described in the Blastocystis secretoma. Similarly, symbiotic coexistence with the intestinal microbiota promotes the survival of parasites facilitating cell invasion and nutrients obtention. Furthermore, it is necessary to identify and characterize more glycosidases, which have been only partially described by in silico analyses of the parasite genome.
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spelling Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoaMucinsLectinsGlycosidasesProtozoaIntestinal parasitesIntestinal mucins are the first line of defense against microorganisms. Although knowledge about the mechanisms involved in the establishment of intestinal protozoa is limited, there is evidence that these parasites produce lectin-like molecules and glycosidases, that exert both, constitutive and secretory functions, promoting the establishment of these microorganisms. In the present review, we analyse the main interactions between mucins of the host intestine and the four main protozoan parasites in humans and their implications in intestinal colonization. There are lectin-like molecules that contain complex oligosaccharide structures and N-acetylglucosamine (GlcNAc), mannose and sialic acid as main components, which are excreted/secreted by Giardia intestinalis, and recognized by the host using mannose-binding lectins (MBL). Entamoeba histolytica and Cryptosporidium spp. express the lectin galactose/N-acetyl-D-galactosamine, which facilitates their adhesion to cells. In Cryptosporidium, the glycoproteins gp30, gp40/15 and gp900 and the glycoprotein lectin CpClec are involved in protozoan adhesion to intestinal cells, forming an adhesion-attack complex. G. intestinalis and E. histolytica can also produce glycosidases such as β-N-acetyl-D-glucosaminidase, α-d-glucosidase, β-d-galactosidase, β-l-fucosidase, α-N-acetyl-d-galactosaminidase and β-mannosidase. In Blastocystis, α-D-mannose, α-D-glucose, GlcNAc, α-D-fucose, chitin and sialic acid that have been identified on their surface. Fucosidases, hexosaminidases and polygalacturonases, which may be involved in the mucin degradation process, have also been described in the Blastocystis secretoma. Similarly, symbiotic coexistence with the intestinal microbiota promotes the survival of parasites facilitating cell invasion and nutrients obtention. Furthermore, it is necessary to identify and characterize more glycosidases, which have been only partially described by in silico analyses of the parasite genome.Universidade de São Paulo. Instituto de Medicina Tropical de São Paulo2020-10-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/xmlapplication/pdfhttps://www.revistas.usp.br/rimtsp/article/view/17593110.1590/s1678-9946202062064Revista do Instituto de Medicina Tropical de São Paulo; Vol. 62 (2020); e64Revista do Instituto de Medicina Tropical de São Paulo; Vol. 62 (2020); e64Revista do Instituto de Medicina Tropical de São Paulo; v. 62 (2020); e641678-99460036-4665reponame:Revista do Instituto de Medicina Tropical de São Pauloinstname:Instituto de Medicina Tropical (IMT)instacron:IMTenghttps://www.revistas.usp.br/rimtsp/article/view/175931/163737https://www.revistas.usp.br/rimtsp/article/view/175931/163736Copyright (c) 2020 Revista do Instituto de Medicina Tropical de São Paulohttp://creativecommons.org/licenses/by-nc/4.0info:eu-repo/semantics/openAccessOlivo-Díaz , AngélicaMartínez-Ocaña, Joel Maravilla, Pablo2020-10-26T17:39:25Zoai:revistas.usp.br:article/175931Revistahttp://www.revistas.usp.br/rimtsp/indexPUBhttps://www.revistas.usp.br/rimtsp/oai||revimtsp@usp.br1678-99460036-4665opendoar:2022-12-13T16:52:53.674058Revista do Instituto de Medicina Tropical de São Paulo - Instituto de Medicina Tropical (IMT)true
dc.title.none.fl_str_mv Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
title Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
spellingShingle Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
Olivo-Díaz , Angélica
Mucins
Lectins
Glycosidases
Protozoa
Intestinal parasites
title_short Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
title_full Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
title_fullStr Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
title_full_unstemmed Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
title_sort Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa
author Olivo-Díaz , Angélica
author_facet Olivo-Díaz , Angélica
Martínez-Ocaña, Joel
Maravilla, Pablo
author_role author
author2 Martínez-Ocaña, Joel
Maravilla, Pablo
author2_role author
author
dc.contributor.author.fl_str_mv Olivo-Díaz , Angélica
Martínez-Ocaña, Joel
Maravilla, Pablo
dc.subject.por.fl_str_mv Mucins
Lectins
Glycosidases
Protozoa
Intestinal parasites
topic Mucins
Lectins
Glycosidases
Protozoa
Intestinal parasites
description Intestinal mucins are the first line of defense against microorganisms. Although knowledge about the mechanisms involved in the establishment of intestinal protozoa is limited, there is evidence that these parasites produce lectin-like molecules and glycosidases, that exert both, constitutive and secretory functions, promoting the establishment of these microorganisms. In the present review, we analyse the main interactions between mucins of the host intestine and the four main protozoan parasites in humans and their implications in intestinal colonization. There are lectin-like molecules that contain complex oligosaccharide structures and N-acetylglucosamine (GlcNAc), mannose and sialic acid as main components, which are excreted/secreted by Giardia intestinalis, and recognized by the host using mannose-binding lectins (MBL). Entamoeba histolytica and Cryptosporidium spp. express the lectin galactose/N-acetyl-D-galactosamine, which facilitates their adhesion to cells. In Cryptosporidium, the glycoproteins gp30, gp40/15 and gp900 and the glycoprotein lectin CpClec are involved in protozoan adhesion to intestinal cells, forming an adhesion-attack complex. G. intestinalis and E. histolytica can also produce glycosidases such as β-N-acetyl-D-glucosaminidase, α-d-glucosidase, β-d-galactosidase, β-l-fucosidase, α-N-acetyl-d-galactosaminidase and β-mannosidase. In Blastocystis, α-D-mannose, α-D-glucose, GlcNAc, α-D-fucose, chitin and sialic acid that have been identified on their surface. Fucosidases, hexosaminidases and polygalacturonases, which may be involved in the mucin degradation process, have also been described in the Blastocystis secretoma. Similarly, symbiotic coexistence with the intestinal microbiota promotes the survival of parasites facilitating cell invasion and nutrients obtention. Furthermore, it is necessary to identify and characterize more glycosidases, which have been only partially described by in silico analyses of the parasite genome.
publishDate 2020
dc.date.none.fl_str_mv 2020-10-07
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://www.revistas.usp.br/rimtsp/article/view/175931
10.1590/s1678-9946202062064
url https://www.revistas.usp.br/rimtsp/article/view/175931
identifier_str_mv 10.1590/s1678-9946202062064
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://www.revistas.usp.br/rimtsp/article/view/175931/163737
https://www.revistas.usp.br/rimtsp/article/view/175931/163736
dc.rights.driver.fl_str_mv Copyright (c) 2020 Revista do Instituto de Medicina Tropical de São Paulo
http://creativecommons.org/licenses/by-nc/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Copyright (c) 2020 Revista do Instituto de Medicina Tropical de São Paulo
http://creativecommons.org/licenses/by-nc/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/xml
application/pdf
dc.publisher.none.fl_str_mv Universidade de São Paulo. Instituto de Medicina Tropical de São Paulo
publisher.none.fl_str_mv Universidade de São Paulo. Instituto de Medicina Tropical de São Paulo
dc.source.none.fl_str_mv Revista do Instituto de Medicina Tropical de São Paulo; Vol. 62 (2020); e64
Revista do Instituto de Medicina Tropical de São Paulo; Vol. 62 (2020); e64
Revista do Instituto de Medicina Tropical de São Paulo; v. 62 (2020); e64
1678-9946
0036-4665
reponame:Revista do Instituto de Medicina Tropical de São Paulo
instname:Instituto de Medicina Tropical (IMT)
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institution IMT
reponame_str Revista do Instituto de Medicina Tropical de São Paulo
collection Revista do Instituto de Medicina Tropical de São Paulo
repository.name.fl_str_mv Revista do Instituto de Medicina Tropical de São Paulo - Instituto de Medicina Tropical (IMT)
repository.mail.fl_str_mv ||revimtsp@usp.br
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