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N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan
Recognition of (1→3)-β-d-glucans (BGs) by invertebrate β-1,3-d-glucan recognition protein (BGRP) plays a significant role in the activation of Toll pathway and prophenoloxidase systems in insect host defense against fungal invasion. To examine the structure diversity of BGRPs for the recognition of...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6678557/ https://www.ncbi.nlm.nih.gov/pubmed/31315292 http://dx.doi.org/10.3390/ijms20143498 |
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author | Adachi, Yoshiyuki Ishii, Masaki Kanno, Takashi Tetsui, Junko Ishibashi, Ken-ichi Yamanaka, Daisuke Miura, Noriko Ohno, Naohito |
author_facet | Adachi, Yoshiyuki Ishii, Masaki Kanno, Takashi Tetsui, Junko Ishibashi, Ken-ichi Yamanaka, Daisuke Miura, Noriko Ohno, Naohito |
author_sort | Adachi, Yoshiyuki |
collection | PubMed |
description | Recognition of (1→3)-β-d-glucans (BGs) by invertebrate β-1,3-d-glucan recognition protein (BGRP) plays a significant role in the activation of Toll pathway and prophenoloxidase systems in insect host defense against fungal invasion. To examine the structure diversity of BGRPs for the recognition of physiochemically different BGs, the binding specificity of BGRPs cloned from four different insects to structure different BGs was characterized using ELISA. Recombinant BGRPs expressed as Fc-fusion proteins of human IgG1 bound to the solid phase of BGs. Based on the binding specificities, the BGRPs were categorized into two groups with different ultrastructures and binding characters; one group specifically binds BGs with triple-helical conformation, while the other group recognizes BGs with disordered conformations like single-helical or partially opened triple helix. The BGRPs from the silkworm and the Indian meal moth bound to the BGs with a triple-helical structure, whereas BGRPs from the red flour beetle and yellow mealworm beetle showed no binding to triple-helical BGs, but bound to alkaline-treated BGs that have a partially opened triple-helical conformation. This evidence suggests that the insect BGRPs can distinguish between different conformations of BGs and are equipped for determining the diversity of BG structures. |
format | Online Article Text |
id | pubmed-6678557 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-66785572019-08-19 N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan Adachi, Yoshiyuki Ishii, Masaki Kanno, Takashi Tetsui, Junko Ishibashi, Ken-ichi Yamanaka, Daisuke Miura, Noriko Ohno, Naohito Int J Mol Sci Article Recognition of (1→3)-β-d-glucans (BGs) by invertebrate β-1,3-d-glucan recognition protein (BGRP) plays a significant role in the activation of Toll pathway and prophenoloxidase systems in insect host defense against fungal invasion. To examine the structure diversity of BGRPs for the recognition of physiochemically different BGs, the binding specificity of BGRPs cloned from four different insects to structure different BGs was characterized using ELISA. Recombinant BGRPs expressed as Fc-fusion proteins of human IgG1 bound to the solid phase of BGs. Based on the binding specificities, the BGRPs were categorized into two groups with different ultrastructures and binding characters; one group specifically binds BGs with triple-helical conformation, while the other group recognizes BGs with disordered conformations like single-helical or partially opened triple helix. The BGRPs from the silkworm and the Indian meal moth bound to the BGs with a triple-helical structure, whereas BGRPs from the red flour beetle and yellow mealworm beetle showed no binding to triple-helical BGs, but bound to alkaline-treated BGs that have a partially opened triple-helical conformation. This evidence suggests that the insect BGRPs can distinguish between different conformations of BGs and are equipped for determining the diversity of BG structures. MDPI 2019-07-16 /pmc/articles/PMC6678557/ /pubmed/31315292 http://dx.doi.org/10.3390/ijms20143498 Text en © 2019 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 Adachi, Yoshiyuki Ishii, Masaki Kanno, Takashi Tetsui, Junko Ishibashi, Ken-ichi Yamanaka, Daisuke Miura, Noriko Ohno, Naohito N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan |
title | N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan |
title_full | N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan |
title_fullStr | N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan |
title_full_unstemmed | N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan |
title_short | N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan |
title_sort | n-terminal (1→3)-β-d-glucan recognition proteins from insects recognize the difference in ultra-structures of (1→3)-β-d-glucan |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6678557/ https://www.ncbi.nlm.nih.gov/pubmed/31315292 http://dx.doi.org/10.3390/ijms20143498 |
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