Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

N-Terminal (1→3)-β-D-glucan Recognition Proteins from Insects Recognize the Difference in ultra-Structures of (1→3)-β-D-glucan

Yoshiyuki Adachi
* ORCID logo ,
Masaki Ishii
ORCID logo ,
Takashi Kanno
,
Junko Tetsui
,
Ken-ichi Ishibashi
ORCID logo ,
Daisuke Yamanaka
,
Noriko Miura
,
Naohito Ohno
Version 1 : Received: 23 May 2019 / Approved: 24 May 2019 / Online: 24 May 2019 (08:56:43 CEST)

A peer-reviewed article of this Preprint also exists.

Adachi, Y.; Ishii, M.; Kanno, T.; Tetsui, J.; Ishibashi, K.; Yamanaka, D.; Miura, N.; Ohno, N. N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan. Int. J. Mol. Sci. 2019, 20, 3498. Adachi, Y.; Ishii, M.; Kanno, T.; Tetsui, J.; Ishibashi, K.; Yamanaka, D.; Miura, N.; Ohno, N. N-Terminal (1→3)-β-d-Glucan Recognition Proteins from Insects Recognize the Difference in Ultra-Structures of (1→3)-β-d-Glucan. Int. J. Mol. Sci. 2019, 20, 3498.

Abstract

The recognition of (1→3)-β-D-glucans (BGs) by β-1,3-D-glucan recognition protein (BGRP) found in invertebrates plays a significant role in the activation of toll pathway and pro-phenol oxidase system in insect host defense against fungal invasion. To examine the structural diversity of BGs in BGRP interaction, the binding specificity of BGRPs cloned from four different insectswas characterized using ELISA. Recombinant BGRPs expressed as Fc-fusion proteins of human IgG1 bound to solid phase BGs. Because of the binding specificities, the BGRPs were categorized into two different ultrastructure- binding characters. The BGRPs from Silkworm and Indian meal moth bound to BGs containing triple-helical structure. Other BGRPs from red flour beetle and yellow mealworm beetle showed no binding to triple-helical BGs, but to alkaline-treated BGs, which have partially opened helical conformation. These evidences suggest that the innate immune system distinguishes different BG conformations and it is equipped for the diversity of BG structures.

Keywords

β-D-glucan; glucan binding protein; host defense; innate immunity

Subject

Biology and Life Sciences, Immunology and Microbiology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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