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Macrobrachium rosenbergii nodavirus virus-like particles attach to fucosylated glycans in the gills of the giant freshwater prawn.
Somrit, Monsicha; Yu, Shin-Yi; Le Pendu, Jacques; Breiman, Adrien; Guérardel, Yann; Weerachatyanukul, Wattana; Watthammawut, Atthaboon.
Afiliação
  • Somrit M; Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
  • Yu SY; CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille, France.
  • Le Pendu J; Inserm, CRCINA, Université de Nantes, Nantes, France.
  • Breiman A; Inserm, CRCINA, Université de Nantes, Nantes, France.
  • Guérardel Y; Centre Hospitalier Universitaire de Nantes, Nantes, France.
  • Weerachatyanukul W; CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, Lille, France.
  • Watthammawut A; Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Cell Microbiol ; 22(12): e13258, 2020 12.
Article em En | MEDLINE | ID: mdl-32862508
ABSTRACT
The Macrobrachium rosenbergii nodavirus (MrNV), the causative agent of white-tail disease (WTD) in many species of shrimp and prawn, has been shown to infect hemocytes and tissues such as the gills and muscles. However, little is known about the host surface molecules to which MrNV attach to initiate infection. Therefore, the present study investigated the role of glycans as binding molecules for virus attachment in susceptible tissues such as the gills. We established that MrNV in their virus-like particle (MrNV-VLP) form exhibited strong binding to gill tissues and lysates, which was highly reduced by the glycan-reducing periodate and PNGase F. The broad, fucose-binding Aleuria Aurantia lectin (AAL) highly reduced MrNV-VLPs binding to gill tissue sections and lysates, and efficiently disrupted the specific interactions between the VLPs and gill glycoproteins. Furthermore, mass spectroscopy revealed the existence of unique fucosylated LacdiNAc-extended N-linked and O-linked glycans in the gill tissues, whereas beta-elimination experiments showed that MrNV-VLPs demonstrated a binding preference for N-glycans. Therefore, the results from this study highly suggested that MrNV-VLPs preferentially attach to fucosylated N-glycans in the susceptible gill tissues, and these findings could lead to the development of strategies that target virus-host surface glycan interactions to reduce MrNV infections.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Polissacarídeos / Nodaviridae / Palaemonidae / Ligação Viral / Fucose / Brânquias Limite: Animals Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Polissacarídeos / Nodaviridae / Palaemonidae / Ligação Viral / Fucose / Brânquias Limite: Animals Idioma: En Ano de publicação: 2020 Tipo de documento: Article