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Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self
Mucosal surfaces are of key importance in protecting animals against external threats including pathogens. In the mucosal surfaces, host molecules interact with non-self to prevent infection and disease. Interestingly, both inhibition and stimulation of uptake hinder infection. In this review, the c...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6100423/ https://www.ncbi.nlm.nih.gov/pubmed/29747390 http://dx.doi.org/10.3390/molecules23051119 |
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author | Brinchmann, Monica Fengsrud Patel, Deepti Manjari Pinto, Nevil Iversen, Martin Haugmo |
author_facet | Brinchmann, Monica Fengsrud Patel, Deepti Manjari Pinto, Nevil Iversen, Martin Haugmo |
author_sort | Brinchmann, Monica Fengsrud |
collection | PubMed |
description | Mucosal surfaces are of key importance in protecting animals against external threats including pathogens. In the mucosal surfaces, host molecules interact with non-self to prevent infection and disease. Interestingly, both inhibition and stimulation of uptake hinder infection. In this review, the current knowledgebase on teleost mucosal lectins’ ability to interact with non-self is summarised with a focus on agglutination, growth inhibition, opsonisation, cell adhesion, and direct killing activities. Further research on lectins is essential, both to understand the immune system of fishes, since they rely more on the innate immune system than mammals, and also to explore these molecules’ antibiotic and antiparasitic activities against veterinary and human pathogens. |
format | Online Article Text |
id | pubmed-6100423 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-61004232018-11-13 Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self Brinchmann, Monica Fengsrud Patel, Deepti Manjari Pinto, Nevil Iversen, Martin Haugmo Molecules Review Mucosal surfaces are of key importance in protecting animals against external threats including pathogens. In the mucosal surfaces, host molecules interact with non-self to prevent infection and disease. Interestingly, both inhibition and stimulation of uptake hinder infection. In this review, the current knowledgebase on teleost mucosal lectins’ ability to interact with non-self is summarised with a focus on agglutination, growth inhibition, opsonisation, cell adhesion, and direct killing activities. Further research on lectins is essential, both to understand the immune system of fishes, since they rely more on the innate immune system than mammals, and also to explore these molecules’ antibiotic and antiparasitic activities against veterinary and human pathogens. MDPI 2018-05-09 /pmc/articles/PMC6100423/ /pubmed/29747390 http://dx.doi.org/10.3390/molecules23051119 Text en © 2018 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 | Review Brinchmann, Monica Fengsrud Patel, Deepti Manjari Pinto, Nevil Iversen, Martin Haugmo Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self |
title | Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self |
title_full | Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self |
title_fullStr | Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self |
title_full_unstemmed | Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self |
title_short | Functional Aspects of Fish Mucosal Lectins—Interaction with Non-Self |
title_sort | functional aspects of fish mucosal lectins—interaction with non-self |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6100423/ https://www.ncbi.nlm.nih.gov/pubmed/29747390 http://dx.doi.org/10.3390/molecules23051119 |
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