A novel defective recombinant porcine enterovirus G virus carrying a porcine torovirus papain-like cysteine protease gene and a putative anti-apoptosis gene in place of viral structural protein genes.

Animals Apoptosis Regulatory Proteins / genetics Cysteine Proteases / genetics Enterovirus Infections / epidemiology Enteroviruses, Porcine / genetics Feces / virology Gene Expression Regulation, Enzymologic Gene Expression Regulation, Viral Phylogeny Swine Swine Diseases / epidemiology Viral Structural Proteins / genetics
Enterovirus Recombination Torovirus

Journal

Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases
ISSN: 1567-7257
Titre abrégé: Infect Genet Evol
Pays: Netherlands
ID NLM: 101084138

Informations de publication

Date de publication:
11 2019
Historique:
received: 18 04 2019
revised: 17 07 2019
accepted: 19 07 2019
pubmed: 26 7 2019
medline: 21 4 2020
entrez: 26 7 2019
Statut: ppublish

Résumé

Enterovirus G (EV-G) belongs to the family of Picornaviridae. Two types of recombinant porcine EV-Gs carrying papain-like cysteine protease (PLCP) gene of porcine torovirus, a virus in Coronaviridae, are reported. Type 1 recombinant EV-Gs are detected in pig feces in Japan, USA, and Belgium and carry the PLPC gene at the junction site of 2C/3A genes, while PLPC gene replaces the viral structural genes in type 2 recombinant EV-G detected in pig feces in a Chinese farm. We identified a novel type 2 recombinant EV-G carrying the PLCP gene with flanking sequences in place of the viral structural genes in pig feces in Japan. The ~0.3 kb-long upstream flanking sequence had no sequence homology with any proteins deposited in GenBank, while the downstream ~0.9 kb-long flanking sequence included a domain having high amino acid sequence homology with a baculoviral inhibitor of apoptosis repeat superfamily. The pig feces, where the novel type 2 recombinant EV-G was detected, also carried type 1 recombinant EV-G. The amount of type 1 and type 2 recombinant EV-G genomes was almost same in the pig feces. Although the phylogenetic analysis suggested that these two recombinant EV-Gs have independently evolved, type 1 recombinant EV-G might have served as a helper virus by providing viral structural proteins for dissemination of the type 2 recombinant EV-G.

Identifiants

DOI: 10.1016/j.meegid.2019.103975 PMID: 31344488 PMC: PMC7105976
pubmed: 31344488
pii: S1567-1348(19)30193-5
doi: 10.1016/j.meegid.2019.103975
pmc: PMC7105976
pii:
doi:

Substances chimiques

Apoptosis Regulatory Proteins 0
Viral Structural Proteins 0
Cysteine Proteases EC 3.4.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

103975

Informations de copyright

Copyright © 2019. Published by Elsevier B.V.

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Auteurs

Ryo Imai (R)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Makoto Nagai (M)

Azabu University, Sagamihara, Kanagawa, Japan. Electronic address: m-nagai@cc.tuat.ac.jp.

Mami Oba (M)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Shoichi Sakaguchi (S)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan; Osaka Medical College, Osaka, Japan.

Makoto Ujike (M)

Laboratory of Veterinary Infectious Diseases, Faculty of Veterinary Medicine, Nippon Veterinary and Life Science University, Musashino, Tokyo, Japan.

Ruka Kimura (R)

Laboratory of Veterinary Infectious Diseases, Faculty of Veterinary Medicine, Nippon Veterinary and Life Science University, Musashino, Tokyo, Japan.

Moeko Kida (M)

Laboratory of Veterinary Infectious Diseases, Faculty of Veterinary Medicine, Nippon Veterinary and Life Science University, Musashino, Tokyo, Japan.

Tsuneyuki Masuda (T)

Kurayoshi Livestock Hygiene Service Center, Kurayoshi, Tottori, Japan.

Moegi Kuroda (M)

Kurayoshi Livestock Hygiene Service Center, Kurayoshi, Tottori, Japan.

Rongduo Wen (R)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Kaixin Li (K)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Yukie Katayama (Y)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Yuki Naoi (Y)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Shinobu Tsuchiaka (S)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Tsutomu Omatsu (T)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.

Hiroshi Yamazato (H)

Kurayoshi Livestock Hygiene Service Center, Kurayoshi, Tottori, Japan.

Shinji Makino (S)

Department of Microbiology and Immunology, The University of Texas Medical Branch at Galveston, Galveston, TX, United States of America.

Tetsuya Mizutani (T)

Research and Education Center for Prevention of Global Infectious Disease of Animal, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan. Electronic address: tmizutan@cc.tuat.ac.jp.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › A novel defective recombinant porcine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › A novel defective recombinant porcine...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Peptide hydrolases › Cysteine proteases › A novel defective recombinant porcine...
questionsmedicales.fr › Infection › Maladies virales › Infections à virus à ARN › Infections à Picornaviridae › Infections à entérovirus › A novel defective recombinant porcine...
questionsmedicales.fr › Virus › Virus à ARN › Virus à ARN à brin positif › Picornaviridae › Enterovirus › Entérovirus porcins › A novel defective recombinant porcine...
questionsmedicales.fr › Liquides et sécrétions biologiques › Fèces › A novel defective recombinant porcine...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes codant pour des enzymes › A novel defective recombinant porcine...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes viraux › A novel defective recombinant porcine...
questionsmedicales.fr › Sciences de l'information › Phylogenèse › A novel defective recombinant porcine...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Artiodactyla › Suidae › A novel defective recombinant porcine...
questionsmedicales.fr › Maladies de l'animal › Maladies des porcs › A novel defective recombinant porcine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales structurales › A novel defective recombinant porcine...