Novel transmembrane receptor involved in phagosome transport of lysozymes and β-hexosaminidase in the enteric protozoan Entamoeba histolytica

古川, 敦; Furukawa, Atsushi; Nakada-Tsukui, Kumiko; Nozaki, Tomoyoshi

doi:10.1371/journal.ppat.1002539

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Novel transmembrane receptor involved in phagosome transport of lysozymes and β-hexosaminidase in the enteric protozoan Entamoeba histolytica

https://doi.org/10.24517/00067083

名前 / ファイル	ライセンス	アクション
PH-PR-FURUKAWA-A-8-1002539.pdf (2.5 MB)

Item type

学術雑誌論文 / Journal Article(1)

公開日

2022-09-12

タイトル

Novel transmembrane receptor involved in phagosome transport of lysozymes and β-hexosaminidase in the enteric protozoan Entamoeba histolytica

言語

eng

資源タイプ

資源タイプ識別子

http://purl.org/coar/resource_type/c_6501

資源タイプ

journal article

ID登録

10.24517/00067083

ID登録タイプ

JaLC

著者

Furukawa, Atsushi

WEKO 106955
e-Rad 30727699

	Furukawa, Atsushi

Search repository

Nakada-Tsukui, Kumiko

Nozaki, Tomoyoshi

著者別表示

古川, 敦

提供者所属

内容記述タイプ

Other

内容記述

金沢大学医薬保健研究域薬学系

書誌情報

PLoS Pathogens

巻 8, 号 2, p. e1002539, 発行日 2012-02

ISSN

収録物識別子タイプ

ISSN

収録物識別子

1553-7366

ISSN

収録物識別子タイプ

ISSN

収録物識別子

1553-7374

DOI

関連識別子

10.1371/journal.ppat.1002539

出版者

Public Library of Science

抄録

内容記述タイプ

Abstract

内容記述

Lysozymes and hexosaminidases are ubiquitous hydrolases in bacteria and eukaryotes. In phagocytic lower eukaryotes and professional phagocytes from higher eukaryotes, they are involved in the degradation of ingested bacteria in phagosomes. In Entamoeba histolytica, which is the intestinal protozoan parasite that causes amoebiasis, phagocytosis plays a pivotal role in the nutrient acquisition and the evasion from the host defense systems. While the content of phagosomes and biochemical and physiological roles of the major phagosomal proteins have been established in E. histolytica, the mechanisms of trafficking of these phagosomal proteins, in general, remain largely unknown. In this study, we identified and characterized for the first time the putative receptor/carrier involved in the transport of the above-mentioned hydrolases to phagosomes. We have shown that the receptor, designated as cysteine protease binding protein family 8 (CPBF8), is localized in lysosomes and mediates transport of lysozymes and β-hexosaminidase α-subunit to phagosomes when the amoeba ingests mammalian cells or Gram-positive bacillus Clostridium perfringens. We have also shown that the binding of CPBF8 to the cargos is mediated by the serine-rich domain, more specifically three serine residues of the domain, which likely contains trifluoroacetic acid-sensitive O-phosphodiester-linked glycan modifications, of CPBF8. We further showed that the repression of CPBF8 by gene silencing reduced the lysozyme and β-hexosaminidase activity in phagosomes and delayed the degradation of C. perfringens. Repression of CPBF8 also resulted in decrease in the cytopathy against the mammalian cells, suggesting that CPBF8 may also be involved in, besides the degradation of ingested bacteria, the pathogenesis against the mammalian hosts. This work represents the first case of the identification of a transport receptor of hydrolytic enzymes responsible for the degradation of microorganisms in phagosomes. © 2012 Furukawa et al.

権利

権利情報

Copyright © 2012 Furukawa et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

権利

権利情報

This is an Open Access article under the CC BY license.

著者版フラグ

出版タイプ

VoR

出版タイプResource

http://purl.org/coar/version/c_970fb48d4fbd8a85