Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Adachi, Yoshiyuki, Ishii, Masaki, Kanno, Takashi, Tetsui, Junko, Ishibashi, Ken-ichi, Yamanaka, Daisuke, Miura, Noriko, Ohno, Naohito
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
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
_version_ 1783441129222438912
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
work_keys_str_mv AT adachiyoshiyuki nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT ishiimasaki nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT kannotakashi nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT tetsuijunko nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT ishibashikenichi nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT yamanakadaisuke nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT miuranoriko nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan
AT ohnonaohito nterminal13bdglucanrecognitionproteinsfrominsectsrecognizethedifferenceinultrastructuresof13bdglucan