Cargando…
A Fish Galectin-8 Possesses Direct Bactericidal Activity
Galectins are a family of animal lectins with high affinity for β-galactosides. Galectins are able to bind to bacteria, and a few mammalian galectins are known to kill the bound bacteria. In fish, no galectins with direct bactericidal effect have been reported. In the present study, we identified an...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7796122/ https://www.ncbi.nlm.nih.gov/pubmed/33396490 http://dx.doi.org/10.3390/ijms22010376 |
_version_ | 1783634606669430784 |
---|---|
author | Zhang, Tengfei Jiang, Shuai Sun, Li |
author_facet | Zhang, Tengfei Jiang, Shuai Sun, Li |
author_sort | Zhang, Tengfei |
collection | PubMed |
description | Galectins are a family of animal lectins with high affinity for β-galactosides. Galectins are able to bind to bacteria, and a few mammalian galectins are known to kill the bound bacteria. In fish, no galectins with direct bactericidal effect have been reported. In the present study, we identified and characterized a tandem repeat galectin-8 from tongue sole Cynoglossus semilaevis (designated CsGal-8). CsGal-8 possesses conserved carbohydrate recognition domains (CRDs), as well as the conserved HXNPR and WGXEE motifs that are critical for carbohydrate binding. CsGal-8 was constitutively expressed in nine tissues of tongue sole and up-regulated in kidney, spleen, and blood by bacterial challenge. When expressed in HeLa cells, CsGal-8 protein was detected both in the cytoplasm and in the micro-vesicles secreted from the cells. Recombinant CsGal-8 (rCsGal-8) bound to lactose and other carbohydrates in a dose dependent manner. rCsGal-8 bound to a wide range of gram-positive and gram-negative bacteria and was co-localized with the bound bacteria in animal cells. Lactose, fructose, galactose, and trehalose effectively blocked the interactions between rCsGal-8 and different bacteria. Furthermore, rCsGal-8 exerted potent bactericidal activity against some gram-negative bacterial pathogens by directly damaging the membrane and structure of the pathogens. Taken together, these results indicate that CsGal-8 likely plays an important role in the immune defense against some bacterial pathogens by direct bacterial interaction and killing. |
format | Online Article Text |
id | pubmed-7796122 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-77961222021-01-10 A Fish Galectin-8 Possesses Direct Bactericidal Activity Zhang, Tengfei Jiang, Shuai Sun, Li Int J Mol Sci Article Galectins are a family of animal lectins with high affinity for β-galactosides. Galectins are able to bind to bacteria, and a few mammalian galectins are known to kill the bound bacteria. In fish, no galectins with direct bactericidal effect have been reported. In the present study, we identified and characterized a tandem repeat galectin-8 from tongue sole Cynoglossus semilaevis (designated CsGal-8). CsGal-8 possesses conserved carbohydrate recognition domains (CRDs), as well as the conserved HXNPR and WGXEE motifs that are critical for carbohydrate binding. CsGal-8 was constitutively expressed in nine tissues of tongue sole and up-regulated in kidney, spleen, and blood by bacterial challenge. When expressed in HeLa cells, CsGal-8 protein was detected both in the cytoplasm and in the micro-vesicles secreted from the cells. Recombinant CsGal-8 (rCsGal-8) bound to lactose and other carbohydrates in a dose dependent manner. rCsGal-8 bound to a wide range of gram-positive and gram-negative bacteria and was co-localized with the bound bacteria in animal cells. Lactose, fructose, galactose, and trehalose effectively blocked the interactions between rCsGal-8 and different bacteria. Furthermore, rCsGal-8 exerted potent bactericidal activity against some gram-negative bacterial pathogens by directly damaging the membrane and structure of the pathogens. Taken together, these results indicate that CsGal-8 likely plays an important role in the immune defense against some bacterial pathogens by direct bacterial interaction and killing. MDPI 2020-12-31 /pmc/articles/PMC7796122/ /pubmed/33396490 http://dx.doi.org/10.3390/ijms22010376 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zhang, Tengfei Jiang, Shuai Sun, Li A Fish Galectin-8 Possesses Direct Bactericidal Activity |
title | A Fish Galectin-8 Possesses Direct Bactericidal Activity |
title_full | A Fish Galectin-8 Possesses Direct Bactericidal Activity |
title_fullStr | A Fish Galectin-8 Possesses Direct Bactericidal Activity |
title_full_unstemmed | A Fish Galectin-8 Possesses Direct Bactericidal Activity |
title_short | A Fish Galectin-8 Possesses Direct Bactericidal Activity |
title_sort | fish galectin-8 possesses direct bactericidal activity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7796122/ https://www.ncbi.nlm.nih.gov/pubmed/33396490 http://dx.doi.org/10.3390/ijms22010376 |
work_keys_str_mv | AT zhangtengfei afishgalectin8possessesdirectbactericidalactivity AT jiangshuai afishgalectin8possessesdirectbactericidalactivity AT sunli afishgalectin8possessesdirectbactericidalactivity AT zhangtengfei fishgalectin8possessesdirectbactericidalactivity AT jiangshuai fishgalectin8possessesdirectbactericidalactivity AT sunli fishgalectin8possessesdirectbactericidalactivity |