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Histamine binding activity of surface-modified yeast by histamine binding protein (HBP)
Histamine is an immune mediator that is mainly secreted when an immediate, rapid response is needed in the body, and an excessive secretion of histamine or lack of enzymes that degrade histamine can result in various side effects. Histamine binding protein (HBP) is secreted by a mite species to prev...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8556473/ https://www.ncbi.nlm.nih.gov/pubmed/34716508 http://dx.doi.org/10.1186/s13568-021-01308-3 |
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author | Jang, Hyeweon Lee, Geun Woo Kim, Yang-Hoon Min, Jiho |
author_facet | Jang, Hyeweon Lee, Geun Woo Kim, Yang-Hoon Min, Jiho |
author_sort | Jang, Hyeweon |
collection | PubMed |
description | Histamine is an immune mediator that is mainly secreted when an immediate, rapid response is needed in the body, and an excessive secretion of histamine or lack of enzymes that degrade histamine can result in various side effects. Histamine binding protein (HBP) is secreted by a mite species to prevent the host’s histamine-induced immune responses by binding the histamine molecule in the blood. Cloning was performed to express HBP on the yeast surface (MBTL-GWL-1), and immunofluorescence (IF) and western blot was performed to confirm the expression of the recombinant protein. The histamine inhibitory ability of GWL-1 cells was tested according to the cell concentration. The highest inhibitory ability of 1.30 × 10(7) CFU/ml of GWL-1 cells was of about 60 %. The GWL-1 cell concentration and the degree of histamine inhibition were confirmed to be dose-dependent, and dead cell debris was shown to have a histamine inhibitory effect, although not as much as that of whole cells. Phagocytosis assays were performed to determine whether histamine affected the RAW 264.7 cell’s phagocytosis, and to indirectly confirm the GWL-1 cell’s histamine inhibition. By confirming that, we found that GWL-1 captures histamine. Therefore, it can be expected to become a competitive material in the anti-allergy market. |
format | Online Article Text |
id | pubmed-8556473 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-85564732021-11-15 Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) Jang, Hyeweon Lee, Geun Woo Kim, Yang-Hoon Min, Jiho AMB Express Original Article Histamine is an immune mediator that is mainly secreted when an immediate, rapid response is needed in the body, and an excessive secretion of histamine or lack of enzymes that degrade histamine can result in various side effects. Histamine binding protein (HBP) is secreted by a mite species to prevent the host’s histamine-induced immune responses by binding the histamine molecule in the blood. Cloning was performed to express HBP on the yeast surface (MBTL-GWL-1), and immunofluorescence (IF) and western blot was performed to confirm the expression of the recombinant protein. The histamine inhibitory ability of GWL-1 cells was tested according to the cell concentration. The highest inhibitory ability of 1.30 × 10(7) CFU/ml of GWL-1 cells was of about 60 %. The GWL-1 cell concentration and the degree of histamine inhibition were confirmed to be dose-dependent, and dead cell debris was shown to have a histamine inhibitory effect, although not as much as that of whole cells. Phagocytosis assays were performed to determine whether histamine affected the RAW 264.7 cell’s phagocytosis, and to indirectly confirm the GWL-1 cell’s histamine inhibition. By confirming that, we found that GWL-1 captures histamine. Therefore, it can be expected to become a competitive material in the anti-allergy market. Springer Berlin Heidelberg 2021-10-29 /pmc/articles/PMC8556473/ /pubmed/34716508 http://dx.doi.org/10.1186/s13568-021-01308-3 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Article Jang, Hyeweon Lee, Geun Woo Kim, Yang-Hoon Min, Jiho Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) |
title | Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) |
title_full | Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) |
title_fullStr | Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) |
title_full_unstemmed | Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) |
title_short | Histamine binding activity of surface-modified yeast by histamine binding protein (HBP) |
title_sort | histamine binding activity of surface-modified yeast by histamine binding protein (hbp) |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8556473/ https://www.ncbi.nlm.nih.gov/pubmed/34716508 http://dx.doi.org/10.1186/s13568-021-01308-3 |
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