Unraveling the role of the MOV10 RNA helicase during influenza A virus infection

Moloney leukemia virus 10 (MOV10) is an interferon-inducible RNA helicase that has been implicated in a broad range of cellular functions, including modulating the replication of a diverse range of viruses. However, the mechanisms by which MOV10 promotes or inhibits the replication of particular vir...

Full description

Saved in:
Bibliographic Details
Published inBiochemical journal Vol. 476; no. 6; p. 1005
Main Authors Villalón-Letelier, Fernando, Reading, Patrick C
Format Journal Article
LanguageEnglish
Published England 27.03.2019
Subjects
Online AccessGet more information

Cover

Loading…
Abstract Moloney leukemia virus 10 (MOV10) is an interferon-inducible RNA helicase that has been implicated in a broad range of cellular functions, including modulating the replication of a diverse range of viruses. However, the mechanisms by which MOV10 promotes or inhibits the replication of particular viruses have not been well defined. A recent paper published in the by Li et al. [Biochem. J. (2019) , 467-481] provides insight regarding the mechanisms by which MOV10 restricts influenza A virus (IAV) infection in host cells. First, the authors confirm that MOV10 binds to the viral nucleoprotein (NP) and sequesters the viral ribonucleoprotein complex in cytoplasmic granules called processing (P)-bodies, thus inhibiting IAV replication. Second, they demonstrate that the non-structural (NS)1 protein of IAV can act as an antagonist of MOV10, inhibiting the association of MOV10 with NP and promoting MOV10 degradation through the lysosomal pathway. Further research will determine if cellular RNA helicases such as MOV10 represent suitable targets for the development of novel anti-IAV therapies.
AbstractList Moloney leukemia virus 10 (MOV10) is an interferon-inducible RNA helicase that has been implicated in a broad range of cellular functions, including modulating the replication of a diverse range of viruses. However, the mechanisms by which MOV10 promotes or inhibits the replication of particular viruses have not been well defined. A recent paper published in the by Li et al. [Biochem. J. (2019) , 467-481] provides insight regarding the mechanisms by which MOV10 restricts influenza A virus (IAV) infection in host cells. First, the authors confirm that MOV10 binds to the viral nucleoprotein (NP) and sequesters the viral ribonucleoprotein complex in cytoplasmic granules called processing (P)-bodies, thus inhibiting IAV replication. Second, they demonstrate that the non-structural (NS)1 protein of IAV can act as an antagonist of MOV10, inhibiting the association of MOV10 with NP and promoting MOV10 degradation through the lysosomal pathway. Further research will determine if cellular RNA helicases such as MOV10 represent suitable targets for the development of novel anti-IAV therapies.
Author Villalón-Letelier, Fernando
Reading, Patrick C
Author_xml – sequence: 1
  givenname: Fernando
  surname: Villalón-Letelier
  fullname: Villalón-Letelier, Fernando
  organization: Department of Microbiology and Immunology, University of Melbourne, Parkville, Victoria 3010, Australia
– sequence: 2
  givenname: Patrick C
  orcidid: 0000-0002-8860-5308
  surname: Reading
  fullname: Reading, Patrick C
  email: preading@unimelb.edu.au
  organization: WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory at The Peter Doherty Institute for Infection and Immunity, 792 Elizabeth St, Melbourne, Victoria 3000, Australia
BackLink https://www.ncbi.nlm.nih.gov/pubmed/30918067$$D View this record in MEDLINE/PubMed
BookMark eNo1j8tOwzAURC0Eog9YsUf-gdBrx4mvlyGiQFUoQoVtZfygQalTOUkl-HpaHqsZHR2NNCNyHJrgCLlgcMVA8Ml1OePAFADDIzJkQkKCkuOAjNr2Y08FCDglgxQUQ8jlkDy9hKh3rq7CO-3WjsamdrTxP_1h8cqAPj8WdL0XjG4dtX08mFXwde_Cl6YF3VWxbw_Ema5qwhk58bpu3flfjslyerMs75L54va-LOaJ4ai6BA3jPveZZN57wQARTI4pSmO89VZnOpfOeKGsBZUZmWpUNrMS05S5DPmYXP7Obvu3jbOrbaw2On6u_p_xb5gyTq4
CitedBy_id crossref_primary_10_3389_fvets_2020_569737
crossref_primary_10_3390_ijms25094677
crossref_primary_10_1186_s13100_024_00324_x
ContentType Journal Article
Copyright 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.
Copyright_xml – notice: 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.
DBID CGR
CUY
CVF
ECM
EIF
NPM
DOI 10.1042/BCJ20190018
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
DatabaseTitleList MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod no_fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
EISSN 1470-8728
ExternalDocumentID 30918067
Genre Comment
Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
-DZ
-~X
0R~
23N
2WC
4.4
53G
5GY
5RE
6J9
79B
A8Z
AABGO
AAHRG
ABPPZ
ABRJW
ACGFO
ACGFS
ACNCT
ADBBV
AEGXH
AENEX
AIAGR
AIZAD
ALMA_UNASSIGNED_HOLDINGS
BAWUL
CGR
CS3
CUY
CVF
DU5
E3Z
EBD
EBS
ECM
EIF
EJD
EMOBN
ESTFP
F5P
H13
HH6
HZ~
K-O
L7B
ML-
MV1
N9A
NPM
NTEUP
O9-
OK1
P2P
RHI
RNS
RPM
RPO
SV3
TR2
TWZ
WH7
XSW
Y6R
YNY
~02
~KM
ID FETCH-LOGICAL-c289t-8c12f6f571fff410880c68387ccfdfda5a67ecf49dd095c73a89d5d78331e582
IngestDate Tue Aug 27 13:47:03 EDT 2024
IsPeerReviewed true
IsScholarly true
Issue 6
Keywords influenza
antiviral
RNA helicase
Language English
License 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c289t-8c12f6f571fff410880c68387ccfdfda5a67ecf49dd095c73a89d5d78331e582
ORCID 0000-0002-8860-5308
PMID 30918067
ParticipantIDs pubmed_primary_30918067
PublicationCentury 2000
PublicationDate 2019-03-27
PublicationDateYYYYMMDD 2019-03-27
PublicationDate_xml – month: 03
  year: 2019
  text: 2019-03-27
  day: 27
PublicationDecade 2010
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle Biochemical journal
PublicationTitleAlternate Biochem J
PublicationYear 2019
References 30617221 - Biochem J. 2019 Feb 5;476(3):467-481
References_xml
SSID ssj0014040
Score 2.355055
Snippet Moloney leukemia virus 10 (MOV10) is an interferon-inducible RNA helicase that has been implicated in a broad range of cellular functions, including modulating...
SourceID pubmed
SourceType Index Database
StartPage 1005
SubjectTerms Cytoplasm
Humans
Infections
Influenza A virus
RNA Helicases
Title Unraveling the role of the MOV10 RNA helicase during influenza A virus infection
URI https://www.ncbi.nlm.nih.gov/pubmed/30918067
Volume 476
hasFullText
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fT9swELYKkwYv08bPjW3yA9rLZEhqO3EeSwVCaJRpKxNvyHFsqaKkiBUk-Ou5s502Yz8Ee4msOG0tf18v5_OdP0K2pbWF1rlgVVZIJuAFxLTjCZPclEKZrlT-iI3jQXZ4Ko7O5Fmn872VtXQzLXfM_R_rSv4HVbgHuGKV7DOQnX0p3IA24AtXQBiuT8L4tEbxoHFT8dRkCmL7-ORHmnz-NuiBK4hxuZ-2qUgcBVmSew024XZ0fTNPyKp_2eEdoZZWOEygPRgU50KlojFuse_xmn0BtxscWY98jEpPZts4IUU_uKqoBXARo7IxzoClTZyFsv0dG2yjyBMwnrGWOxpPEdRbIkvapjBNfD317zYazARmnveP8FdQFLD9FEzw1aWHi4Mno5Kg1fHv3kcHZjddC2QhV6jmMcAATtxYEmC0YpkmjGO3NYpl8rL55KMlhnc1hq_Jq7hGoL0A-BvSsfUKWe3Vejq5vKOfqM_a9dshK2Sp3yj2rZKvcz5Q4ABFPtCJ823PBwp8oA0faOADnfGB9qjnA53xYY0MD_aH_UMWFTOYgYXzlCmTdl3mZJ4650QKb5DEZIqr3BhXuUpLneXWOFFUFbjWJudaFZWscsV5aqXqrpPFelLbTUK7RpVFqpWAp8CscwVuoChLZYVBIcrsLdkIU3R-FU5FOW8m791fe7bI8pxY78kLB39D-wF8umn50aP0ABORSS0
link.rule.ids 780
linkProvider National Library of Medicine
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Unraveling+the+role+of+the+MOV10+RNA+helicase+during+influenza+A+virus+infection&rft.jtitle=Biochemical+journal&rft.au=Villal%C3%B3n-Letelier%2C+Fernando&rft.au=Reading%2C+Patrick+C&rft.date=2019-03-27&rft.eissn=1470-8728&rft.volume=476&rft.issue=6&rft.spage=1005&rft_id=info:doi/10.1042%2FBCJ20190018&rft_id=info%3Apmid%2F30918067&rft_id=info%3Apmid%2F30918067&rft.externalDocID=30918067