Cellular PSMB4 Protein Suppresses Influenza A Virus Replication through Targeting NS1 Protein

The nonstructural protein 1 (NS1) of influenza A virus (IAV) possesses multiple functions, such as the inhibition of the host antiviral immune responses, to facilitate viral infection. To search for cellular proteins interacting with the IAV NS1 protein, the yeast two-hybrid system was adopted. Prot...

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Published inViruses Vol. 14; no. 10; p. 2277
Main Authors Yang, Chee-Hing, Hsu, Che-Fang, Lai, Xiang-Qing, Chan, Yu-Ru, Li, Hui-Chun, Lo, Shih-Yen
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 01.10.2022
MDPI
Subjects
Antiviral drugs
Cellular proteins
Cloning
Confocal microscopy
Development and progression
Experiments
Gene expression
Immune response
Immunoprecipitation
Infections
Influenza
Influenza A
influenza A virus
Interferon
Kinases
Mammalian cells
MG132
Monoclonal antibodies
NS1 protein
Physiological aspects
Plasmids
Proteasomes
protein degradation
Proteins
PSMB4
Replication
Viral infections
Viral proteins
Virus research
Taiwan
United States > US
Germany
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Abstract The nonstructural protein 1 (NS1) of influenza A virus (IAV) possesses multiple functions, such as the inhibition of the host antiviral immune responses, to facilitate viral infection. To search for cellular proteins interacting with the IAV NS1 protein, the yeast two-hybrid system was adopted. Proteasome family member PSMB4 (proteasome subunit beta type 4) was found to interact with the NS1 protein in this screening experiment. The binding domains of these two proteins were also determined using this system. The physical interactions between the NS1 and cellular PSMB4 proteins were further confirmed by co-immunoprecipitation assay and confocal microscopy in mammalian cells. Neither transiently nor stably expressed NS1 protein affected the PSMB4 expression in cells. In contrast, PSMB4 reduced the NS1 protein expression level, especially in the presence of MG132. As expected, the functions of the NS1 protein, such as inhibition of interferon activity and enhancement of transient gene expression, were suppressed by PSMB4. PSMB4 knockdown enhances IAV replication, while its overexpression attenuates IAV replication. Thus, the results of this study suggest that the cellular PSMB4 protein interacts with and possibly facilitates the degradation of the NS1 protein, which in turn suppresses IAV replication.
AbstractList The nonstructural protein 1 (NS1) of influenza A virus (IAV) possesses multiple functions, such as the inhibition of the host antiviral immune responses, to facilitate viral infection. To search for cellular proteins interacting with the IAV NS1 protein, the yeast two-hybrid system was adopted. Proteasome family member PSMB4 (proteasome subunit beta type 4) was found to interact with the NS1 protein in this screening experiment. The binding domains of these two proteins were also determined using this system. The physical interactions between the NS1 and cellular PSMB4 proteins were further confirmed by co-immunoprecipitation assay and confocal microscopy in mammalian cells. Neither transiently nor stably expressed NS1 protein affected the PSMB4 expression in cells. In contrast, PSMB4 reduced the NS1 protein expression level, especially in the presence of MG132. As expected, the functions of the NS1 protein, such as inhibition of interferon activity and enhancement of transient gene expression, were suppressed by PSMB4. PSMB4 knockdown enhances IAV replication, while its overexpression attenuates IAV replication. Thus, the results of this study suggest that the cellular PSMB4 protein interacts with and possibly facilitates the degradation of the NS1 protein, which in turn suppresses IAV replication.The nonstructural protein 1 (NS1) of influenza A virus (IAV) possesses multiple functions, such as the inhibition of the host antiviral immune responses, to facilitate viral infection. To search for cellular proteins interacting with the IAV NS1 protein, the yeast two-hybrid system was adopted. Proteasome family member PSMB4 (proteasome subunit beta type 4) was found to interact with the NS1 protein in this screening experiment. The binding domains of these two proteins were also determined using this system. The physical interactions between the NS1 and cellular PSMB4 proteins were further confirmed by co-immunoprecipitation assay and confocal microscopy in mammalian cells. Neither transiently nor stably expressed NS1 protein affected the PSMB4 expression in cells. In contrast, PSMB4 reduced the NS1 protein expression level, especially in the presence of MG132. As expected, the functions of the NS1 protein, such as inhibition of interferon activity and enhancement of transient gene expression, were suppressed by PSMB4. PSMB4 knockdown enhances IAV replication, while its overexpression attenuates IAV replication. Thus, the results of this study suggest that the cellular PSMB4 protein interacts with and possibly facilitates the degradation of the NS1 protein, which in turn suppresses IAV replication.
The nonstructural protein 1 (NS1) of influenza A virus (IAV) possesses multiple functions, such as the inhibition of the host antiviral immune responses, to facilitate viral infection. To search for cellular proteins interacting with the IAV NS1 protein, the yeast two-hybrid system was adopted. Proteasome family member PSMB4 (proteasome subunit beta type 4) was found to interact with the NS1 protein in this screening experiment. The binding domains of these two proteins were also determined using this system. The physical interactions between the NS1 and cellular PSMB4 proteins were further confirmed by co-immunoprecipitation assay and confocal microscopy in mammalian cells. Neither transiently nor stably expressed NS1 protein affected the PSMB4 expression in cells. In contrast, PSMB4 reduced the NS1 protein expression level, especially in the presence of MG132. As expected, the functions of the NS1 protein, such as inhibition of interferon activity and enhancement of transient gene expression, were suppressed by PSMB4. PSMB4 knockdown enhances IAV replication, while its overexpression attenuates IAV replication. Thus, the results of this study suggest that the cellular PSMB4 protein interacts with and possibly facilitates the degradation of the NS1 protein, which in turn suppresses IAV replication.
Audience Academic
Author Lai, Xiang-Qing
Lo, Shih-Yen
Hsu, Che-Fang
Li, Hui-Chun
Yang, Chee-Hing
Chan, Yu-Ru
AuthorAffiliation 2 Center for Prevention and Therapy of Gynecological Cancers, Department of Medical Research, Hualien Tzu Chi Hospital, Buddhist Tzu Chi Medical Foundation, Hualien 97004, Taiwan
4 Department of Laboratory Medicine, Buddhist Tzu Chi General Hospital, Hualien 97004, Taiwan
3 Department of Biochemistry, Tzu Chi University, Hualien 97004, Taiwan
1 Department of Laboratory Medicine and Biotechnology, Tzu Chi University, No. 701, Section 3, Chung Yang Road, Hualien 97004, Taiwan
AuthorAffiliation_xml – name: 1 Department of Laboratory Medicine and Biotechnology, Tzu Chi University, No. 701, Section 3, Chung Yang Road, Hualien 97004, Taiwan
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– name: 4 Department of Laboratory Medicine, Buddhist Tzu Chi General Hospital, Hualien 97004, Taiwan
– name: 3 Department of Biochemistry, Tzu Chi University, Hualien 97004, Taiwan
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  surname: Yang
  fullname: Yang, Chee-Hing
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CitedBy_id crossref_primary_10_3390_pathogens13020127
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Snippet The nonstructural protein 1 (NS1) of influenza A virus (IAV) possesses multiple functions, such as the inhibition of the host antiviral immune responses, to...
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SubjectTerms Antiviral drugs
Cellular proteins
Cloning
Confocal microscopy
Development and progression
Experiments
Gene expression
Immune response
Immunoprecipitation
Infections
Influenza
Influenza A
influenza A virus
Interferon
Kinases
Mammalian cells
MG132
Monoclonal antibodies
NS1 protein
Physiological aspects
Plasmids
Proteasomes
protein degradation
Proteins
PSMB4
Replication
Viral infections
Viral proteins
Virus research
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Title Cellular PSMB4 Protein Suppresses Influenza A Virus Replication through Targeting NS1 Protein
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https://pubmed.ncbi.nlm.nih.gov/PMC9612107
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Volume 14
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