StressCovidV1, PubMed, Checkpoint, bibRecord, 000311

Proteome Response of Chicken Embryo Fibroblast Cells to Recombinant H5N1 Avian Influenza Viruses with Different Neuraminidase Stalk Lengths.

Identifieur interne : 000311 ( PubMed/Checkpoint ); précédent : 000310; suivant : 000312

Proteome Response of Chicken Embryo Fibroblast Cells to Recombinant H5N1 Avian Influenza Viruses with Different Neuraminidase Stalk Lengths.

Auteurs : Yongtao Li [République populaire de Chine] ; Fan Ming [République populaire de Chine] ; Huimin Huang [République populaire de Chine] ; Kelei Guo [République populaire de Chine] ; Huanchun Chen [République populaire de Chine] ; Meilin Jin [République populaire de Chine] ; Hongbo Zhou [République populaire de Chine]

Source :

Scientific reports [ 2045-2322 ] ; 2017.

RBID : pubmed:28079188

Descripteurs français

KwdFr :
- Animaux, Cartes d'interactions protéiques, Cartographie d'interactions entre protéines, Embryon de poulet, Fibroblastes (métabolisme), Fibroblastes (virologie), Grippe chez les oiseaux (métabolisme), Grippe chez les oiseaux (virologie), Interactions hôte-pathogène, Interféron gamma (pharmacologie), Poulets, Protéome, Protéomique (), Recombinaison génétique, Réplication virale, Sialidase (génétique), Sous-type H5N1 du virus de la grippe A (), Sous-type H5N1 du virus de la grippe A (génétique), Sous-type H5N1 du virus de la grippe A (métabolisme), Sous-type H5N1 du virus de la grippe A (pathogénicité), Transduction du signal.
MESH :
- génétique : Sialidase, Sous-type H5N1 du virus de la grippe A.
- métabolisme : Fibroblastes, Grippe chez les oiseaux, Sous-type H5N1 du virus de la grippe A.
- pathogénicité : Sous-type H5N1 du virus de la grippe A.
- pharmacologie : Interféron gamma.
- virologie : Fibroblastes, Grippe chez les oiseaux.
- Animaux, Cartes d'interactions protéiques, Cartographie d'interactions entre protéines, Embryon de poulet, Interactions hôte-pathogène, Poulets, Protéome, Protéomique, Recombinaison génétique, Réplication virale, Sous-type H5N1 du virus de la grippe A, Transduction du signal.

English descriptors

KwdEn :
- Animals, Chick Embryo, Chickens, Fibroblasts (metabolism), Fibroblasts (virology), Host-Pathogen Interactions, Influenza A Virus, H5N1 Subtype (drug effects), Influenza A Virus, H5N1 Subtype (genetics), Influenza A Virus, H5N1 Subtype (metabolism), Influenza A Virus, H5N1 Subtype (pathogenicity), Influenza in Birds (metabolism), Influenza in Birds (virology), Interferon-gamma (pharmacology), Neuraminidase (genetics), Protein Interaction Mapping, Protein Interaction Maps, Proteome, Proteomics (methods), Recombination, Genetic, Signal Transduction, Virus Replication.
MESH :
- chemical , genetics : Neuraminidase.
- chemical , pharmacology : Interferon-gamma.
- drug effects : Influenza A Virus, H5N1 Subtype.
- genetics : Influenza A Virus, H5N1 Subtype.
- metabolism : Fibroblasts, Influenza A Virus, H5N1 Subtype, Influenza in Birds.
- methods : Proteomics.
- pathogenicity : Influenza A Virus, H5N1 Subtype.
- virology : Fibroblasts, Influenza in Birds.
- Animals, Chick Embryo, Chickens, Host-Pathogen Interactions, Protein Interaction Mapping, Protein Interaction Maps, Proteome, Recombination, Genetic, Signal Transduction, Virus Replication.

Abstract

The variation on neuraminidase (NA) stalk region of highly pathogenic avian influenza H5N1 virus results in virulence change in animals. In our previous studies, the special NA stalk-motif of H5N1 viruses has been demonstrated to play a significant role in the high virulence and pathogenicity in chickens. However, the molecular mechanisms underlying the pathogenicity of viruses with different NA stalk remain poorly understood. This study presents a comprehensive characterization of the proteome response of chicken cells to recombinant H5N1 virus with stalk-short NA (rNA-wt) and the stalkless NA mutant virus (rSD20). 208 proteins with differential abundance profiles were identified differentially expressed (DE), and these proteins were mainly related to stress response, transcription regulation, transport, metabolic process, cellular component and cytoskeleton. Through Ingenuity Pathways Analysis (IPA), the significant biological functions of DE proteins represented included Post-Translational Modification, Protein Folding, DNA Replication, Recombination and Repair. It was interesting to find that most DE proteins were involved in the TGF-β mediated functional network. Moreover, the specific DE proteins may play important roles in the innate immune responses and H5N1 virus replication. Our data provide important information regarding the comparable host response to H5N1 influenza virus infection with different NA stalk lengths.

DOI: 10.1038/srep40698
PubMed: 28079188

Affiliations:

République populaire de Chine

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000328
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Le document en format XML

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<term>Cartes d'interactions protéiques</term>
<term>Cartographie d'interactions entre protéines</term>
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<term>Fibroblastes (métabolisme)</term>
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<term>Protéomique ()</term>
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<term>Réplication virale</term>
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<term>Sous-type H5N1 du virus de la grippe A (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">The variation on neuraminidase (NA) stalk region of highly pathogenic avian influenza H5N1 virus results in virulence change in animals. In our previous studies, the special NA stalk-motif of H5N1 viruses has been demonstrated to play a significant role in the high virulence and pathogenicity in chickens. However, the molecular mechanisms underlying the pathogenicity of viruses with different NA stalk remain poorly understood. This study presents a comprehensive characterization of the proteome response of chicken cells to recombinant H5N1 virus with stalk-short NA (rNA-wt) and the stalkless NA mutant virus (rSD20). 208 proteins with differential abundance profiles were identified differentially expressed (DE), and these proteins were mainly related to stress response, transcription regulation, transport, metabolic process, cellular component and cytoskeleton. Through Ingenuity Pathways Analysis (IPA), the significant biological functions of DE proteins represented included Post-Translational Modification, Protein Folding, DNA Replication, Recombination and Repair. It was interesting to find that most DE proteins were involved in the TGF-β mediated functional network. Moreover, the specific DE proteins may play important roles in the innate immune responses and H5N1 virus replication. Our data provide important information regarding the comparable host response to H5N1 influenza virus infection with different NA stalk lengths.</div>
</front>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28079188</PMID>
<DateCompleted><Year>2018</Year>
<Month>10</Month>
<Day>18</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
<PubDate><Year>2017</Year>
<Month>01</Month>
<Day>12</Day>
</PubDate>
</JournalIssue>
<Title>Scientific reports</Title>
<ISOAbbreviation>Sci Rep</ISOAbbreviation>
</Journal>
<ArticleTitle>Proteome Response of Chicken Embryo Fibroblast Cells to Recombinant H5N1 Avian Influenza Viruses with Different Neuraminidase Stalk Lengths.</ArticleTitle>
<Pagination><MedlinePgn>40698</MedlinePgn>
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<ELocationID EIdType="doi" ValidYN="Y">10.1038/srep40698</ELocationID>
<Abstract><AbstractText>The variation on neuraminidase (NA) stalk region of highly pathogenic avian influenza H5N1 virus results in virulence change in animals. In our previous studies, the special NA stalk-motif of H5N1 viruses has been demonstrated to play a significant role in the high virulence and pathogenicity in chickens. However, the molecular mechanisms underlying the pathogenicity of viruses with different NA stalk remain poorly understood. This study presents a comprehensive characterization of the proteome response of chicken cells to recombinant H5N1 virus with stalk-short NA (rNA-wt) and the stalkless NA mutant virus (rSD20). 208 proteins with differential abundance profiles were identified differentially expressed (DE), and these proteins were mainly related to stress response, transcription regulation, transport, metabolic process, cellular component and cytoskeleton. Through Ingenuity Pathways Analysis (IPA), the significant biological functions of DE proteins represented included Post-Translational Modification, Protein Folding, DNA Replication, Recombination and Repair. It was interesting to find that most DE proteins were involved in the TGF-β mediated functional network. Moreover, the specific DE proteins may play important roles in the innate immune responses and H5N1 virus replication. Our data provide important information regarding the comparable host response to H5N1 influenza virus infection with different NA stalk lengths.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Yongtao</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, 430070, P.R. China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>College of Animal Husbandry &Veterinary Science, Henan Agricultural University, Zhengzhou, 450002, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ming</LastName>
<ForeName>Fan</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, 430070, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Huang</LastName>
<ForeName>Huimin</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, 430070, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Guo</LastName>
<ForeName>Kelei</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, 430070, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Huanchun</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, 430070, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jin</LastName>
<ForeName>Meilin</ForeName>
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<affiliations><list><country><li>République populaire de Chine</li>
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Proteome Response of Chicken Embryo Fibroblast Cells to Recombinant H5N1 Avian Influenza Viruses with Different Neuraminidase Stalk Lengths.

Proteome Response of Chicken Embryo Fibroblast Cells to Recombinant H5N1 Avian Influenza Viruses with Different Neuraminidase Stalk Lengths.

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