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First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein

INTRODUCTION: Animal trade favors the spreading of emerging canine adenovirus 1 (CAdV-1) in mink. Because the 100K protein is not exposed to the viral surface at any stage, it can be used to differentiate the vaccine from wild virus infection. However, no related research has been conducted. This st...

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Autores principales: Hou, Jinyu, Xu, Jinfeng, Wang, Ben, Zhang, Hongling, Yin, Baishuang, Li, Goujiang, Lei, Fashou, Cai, Xiaoming, Zhu, Yanzhu, Wang, Longtao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10469754/
https://www.ncbi.nlm.nih.gov/pubmed/37664114
http://dx.doi.org/10.3389/fmicb.2023.1245581
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author Hou, Jinyu
Xu, Jinfeng
Wang, Ben
Zhang, Hongling
Yin, Baishuang
Li, Goujiang
Lei, Fashou
Cai, Xiaoming
Zhu, Yanzhu
Wang, Longtao
author_facet Hou, Jinyu
Xu, Jinfeng
Wang, Ben
Zhang, Hongling
Yin, Baishuang
Li, Goujiang
Lei, Fashou
Cai, Xiaoming
Zhu, Yanzhu
Wang, Longtao
author_sort Hou, Jinyu
collection PubMed
description INTRODUCTION: Animal trade favors the spreading of emerging canine adenovirus 1 (CAdV-1) in mink. Because the 100K protein is not exposed to the viral surface at any stage, it can be used to differentiate the vaccine from wild virus infection. However, no related research has been conducted. This study aimed to find evidence of CAdV-1 in mink and predict the character of the 100K protein in the current circulating CAdV-1 strain of mink. METHOD: In this experiment, the identification of CAdV-1, the phylogenetic tree, homology, and bioinformatics analysis of 100K were conducted. RESULTS: The results showed that the CAdV-1 was identified in the mink and that its Fiber was located in a separate branch. It was closely related to strains isolated from Norwegian Arctic fox and Red fox. 100K was located in a separate branch, which had the closest genetic relationship with skunks, porcupines, raccoons, and hedgehogs and a far genetic relationship with the strains in dogs. 100K protein is an unstable and hydrophobic protein. It had evidence of selective pressure and recombination, 1 glycosylation site, 48 phosphorylation sites, 60 dominant B cell epitopes, and 9 peptides of MHC-I and MHC-II. Its subcellular localization was mainly in the endoplasmic reticulum and mitochondria. The binding sites of 100K proteins were DBP proteins and 33K proteins. DISCUSSION: The stains in the mink were different from fox. The exploration of its genomic characteristics will provide us with a deeper understanding of the prevention of canine adenovirus.
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spelling pubmed-104697542023-09-01 First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein Hou, Jinyu Xu, Jinfeng Wang, Ben Zhang, Hongling Yin, Baishuang Li, Goujiang Lei, Fashou Cai, Xiaoming Zhu, Yanzhu Wang, Longtao Front Microbiol Microbiology INTRODUCTION: Animal trade favors the spreading of emerging canine adenovirus 1 (CAdV-1) in mink. Because the 100K protein is not exposed to the viral surface at any stage, it can be used to differentiate the vaccine from wild virus infection. However, no related research has been conducted. This study aimed to find evidence of CAdV-1 in mink and predict the character of the 100K protein in the current circulating CAdV-1 strain of mink. METHOD: In this experiment, the identification of CAdV-1, the phylogenetic tree, homology, and bioinformatics analysis of 100K were conducted. RESULTS: The results showed that the CAdV-1 was identified in the mink and that its Fiber was located in a separate branch. It was closely related to strains isolated from Norwegian Arctic fox and Red fox. 100K was located in a separate branch, which had the closest genetic relationship with skunks, porcupines, raccoons, and hedgehogs and a far genetic relationship with the strains in dogs. 100K protein is an unstable and hydrophobic protein. It had evidence of selective pressure and recombination, 1 glycosylation site, 48 phosphorylation sites, 60 dominant B cell epitopes, and 9 peptides of MHC-I and MHC-II. Its subcellular localization was mainly in the endoplasmic reticulum and mitochondria. The binding sites of 100K proteins were DBP proteins and 33K proteins. DISCUSSION: The stains in the mink were different from fox. The exploration of its genomic characteristics will provide us with a deeper understanding of the prevention of canine adenovirus. Frontiers Media S.A. 2023-08-17 /pmc/articles/PMC10469754/ /pubmed/37664114 http://dx.doi.org/10.3389/fmicb.2023.1245581 Text en Copyright © 2023 Hou, Xu, Wang, Zhang, Yin, Li, Lei, Cai, Zhu and Wang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Hou, Jinyu
Xu, Jinfeng
Wang, Ben
Zhang, Hongling
Yin, Baishuang
Li, Goujiang
Lei, Fashou
Cai, Xiaoming
Zhu, Yanzhu
Wang, Longtao
First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein
title First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein
title_full First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein
title_fullStr First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein
title_full_unstemmed First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein
title_short First identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 K protein
title_sort first identification of canine adenovirus 1 in mink and bioinformatics analysis of its 100 k protein
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10469754/
https://www.ncbi.nlm.nih.gov/pubmed/37664114
http://dx.doi.org/10.3389/fmicb.2023.1245581
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