White spot syndrome virus protein kinase 1 defeats the host cell's iron-withholding defense mechanism by interacting with host ferritin
Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nut...
Saved in:
Published in | Journal of virology Vol. 89; no. 2; pp. 1083 - 1093 |
---|---|
Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Microbiology
15.01.2015
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nutrient to the invading pathogens. However, pathogens use various strategies to overcome this host defense. In this study, we demonstrated that white spot syndrome virus (WSSV) protein kinase 1 (PK1) interacted with shrimp ferritin in the yeast two-hybrid system. A pulldown assay and 27-MHz quartz crystal microbalance (QCM) analysis confirmed the interaction between PK1 and both ferritin and apoferritin. PK1 did not promote the release of iron ions from ferritin, but it prevented apoferritin from binding ferrous ions. When PK1 was overexpressed in Sf9 cells, the cellular labile iron pool (LIP) levels were elevated significantly. Immunoprecipitation and atomic absorption spectrophotometry (AAS) further showed that the number of iron ions bound by ferritin decreased significantly at 24 h post-WSSV infection. Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell's iron-withholding defense mechanism.
We show here that white spot syndrome virus (WSSV) ensures the availability of iron by using a previously unreported mechanism to defeat the host cell's iron-withholding defense mechanism. This defense is often implemented by ferritin, which can bind up to 4,500 iron atoms and acts to sequester free iron within the cell. WSSV's novel counterstrategy is mediated by a direct protein-protein interaction between viral protein kinase 1 (PK1) and host ferritin. PK1 interacts with both ferritin and apoferritin, suppresses apoferritin's ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. |
---|---|
AbstractList | Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nutrient to the invading pathogens. However, pathogens use various strategies to overcome this host defense. In this study, we demonstrated that white spot syndrome virus (WSSV) protein kinase 1 (PK1) interacted with shrimp ferritin in the yeast two-hybrid system. A pulldown assay and 27-MHz quartz crystal microbalance (QCM) analysis confirmed the interaction between PK1 and both ferritin and apoferritin. PK1 did not promote the release of iron ions from ferritin, but it prevented apoferritin from binding ferrous ions. When PK1 was overexpressed in Sf9 cells, the cellular labile iron pool (LIP) levels were elevated significantly. Immunoprecipitation and atomic absorption spectrophotometry (AAS) further showed that the number of iron ions bound by ferritin decreased significantly at 24 h post-WSSV infection. Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell's iron-withholding defense mechanism.
We show here that white spot syndrome virus (WSSV) ensures the availability of iron by using a previously unreported mechanism to defeat the host cell's iron-withholding defense mechanism. This defense is often implemented by ferritin, which can bind up to 4,500 iron atoms and acts to sequester free iron within the cell. WSSV's novel counterstrategy is mediated by a direct protein-protein interaction between viral protein kinase 1 (PK1) and host ferritin. PK1 interacts with both ferritin and apoferritin, suppresses apoferritin's ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. ABSTRACT Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nutrient to the invading pathogens. However, pathogens use various strategies to overcome this host defense. In this study, we demonstrated that white spot syndrome virus (WSSV) protein kinase 1 (PK1) interacted with shrimp ferritin in the yeast two-hybrid system. A pulldown assay and 27-MHz quartz crystal microbalance (QCM) analysis confirmed the interaction between PK1 and both ferritin and apoferritin. PK1 did not promote the release of iron ions from ferritin, but it prevented apoferritin from binding ferrous ions. When PK1 was overexpressed in Sf9 cells, the cellular labile iron pool (LIP) levels were elevated significantly. Immunoprecipitation and atomic absorption spectrophotometry (AAS) further showed that the number of iron ions bound by ferritin decreased significantly at 24 h post-WSSV infection. Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell's iron-withholding defense mechanism. IMPORTANCE We show here that white spot syndrome virus (WSSV) ensures the availability of iron by using a previously unreported mechanism to defeat the host cell's iron-withholding defense mechanism. This defense is often implemented by ferritin, which can bind up to 4,500 iron atoms and acts to sequester free iron within the cell. WSSV's novel counterstrategy is mediated by a direct protein-protein interaction between viral protein kinase 1 (PK1) and host ferritin. PK1 interacts with both ferritin and apoferritin, suppresses apoferritin's ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. UNLABELLEDIron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nutrient to the invading pathogens. However, pathogens use various strategies to overcome this host defense. In this study, we demonstrated that white spot syndrome virus (WSSV) protein kinase 1 (PK1) interacted with shrimp ferritin in the yeast two-hybrid system. A pulldown assay and 27-MHz quartz crystal microbalance (QCM) analysis confirmed the interaction between PK1 and both ferritin and apoferritin. PK1 did not promote the release of iron ions from ferritin, but it prevented apoferritin from binding ferrous ions. When PK1 was overexpressed in Sf9 cells, the cellular labile iron pool (LIP) levels were elevated significantly. Immunoprecipitation and atomic absorption spectrophotometry (AAS) further showed that the number of iron ions bound by ferritin decreased significantly at 24 h post-WSSV infection. Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell's iron-withholding defense mechanism.IMPORTANCEWe show here that white spot syndrome virus (WSSV) ensures the availability of iron by using a previously unreported mechanism to defeat the host cell's iron-withholding defense mechanism. This defense is often implemented by ferritin, which can bind up to 4,500 iron atoms and acts to sequester free iron within the cell. WSSV's novel counterstrategy is mediated by a direct protein-protein interaction between viral protein kinase 1 (PK1) and host ferritin. PK1 interacts with both ferritin and apoferritin, suppresses apoferritin's ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nutrient to the invading pathogens. However, pathogens use various strategies to overcome this host defense. In this study, we demonstrated that white spot syndrome virus (WSSV) protein kinase 1 (PK1) interacted with shrimp ferritin in the yeast two-hybrid system. A pulldown assay and 27-MHz quartz crystal microbalance (QCM) analysis confirmed the interaction between PK1 and both ferritin and apoferritin. PK1 did not promote the release of iron ions from ferritin, but it prevented apoferritin from binding ferrous ions. When PK1 was overexpressed in Sf9 cells, the cellular labile iron pool (LIP) levels were elevated significantly. Immunoprecipitation and atomic absorption spectrophotometry (AAS) further showed that the number of iron ions bound by ferritin decreased significantly at 24 h post-WSSV infection. Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell's iron-withholding defense mechanism. IMPORTANCE We show here that white spot syndrome virus (WSSV) ensures the availability of iron by using a previously unreported mechanism to defeat the host cell's iron-withholding defense mechanism. This defense is often implemented by ferritin, which can bind up to 4,500 iron atoms and acts to sequester free iron within the cell. WSSV's novel counterstrategy is mediated by a direct protein-protein interaction between viral protein kinase 1 (PK1) and host ferritin. PK1 interacts with both ferritin and apoferritin, suppresses apoferritin's ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell, and in the event of a pathogenic invasion, the host can use an iron-withholding mechanism to restrict the availability of this essential nutrient to the invading pathogens. However, pathogens use various strategies to overcome this host defense. In this study, we demonstrated that white spot syndrome virus (WSSV) protein kinase 1 (PK1) interacted with shrimp ferritin in the yeast two-hybrid system. A pulldown assay and 27-MHz quartz crystal microbalance (QCM) analysis confirmed the interaction between PK1 and both ferritin and apoferritin. PK1 did not promote the release of iron ions from ferritin, but it prevented apoferritin from binding ferrous ions. When PK1 was overexpressed in Sf9 cells, the cellular labile iron pool (LIP) levels were elevated significantly. Immunoprecipitation and atomic absorption spectrophotometry (AAS) further showed that the number of iron ions bound by ferritin decreased significantly at 24 h post-WSSV infection. Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell's iron-withholding defense mechanism. IMPORTANCE We show here that white spot syndrome virus (WSSV) ensures the availability of iron by using a previously unreported mechanism to defeat the host cell's iron-withholding defense mechanism. This defense is often implemented by ferritin, which can bind up to 4,500 iron atoms and acts to sequester free iron within the cell. WSSV's novel counterstrategy is mediated by a direct protein-protein interaction between viral protein kinase 1 (PK1) and host ferritin. PK1 interacts with both ferritin and apoferritin, suppresses apoferritin's ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. |
Author | Hwang, Pung-Pung Lee, Der-Yen Wang, Hao-Ching Kou, Guang-Hsiung Chang, Geen-Dong Kang, Shih-Ting Huang, Ming-Fen Lo, Chu-Fang Lin, Shin-Jen |
Author_xml | – sequence: 1 givenname: Shin-Jen surname: Lin fullname: Lin, Shin-Jen organization: Institute of Bioinformatics and Biosignal Transduction, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan Department of Life Science, College of Life Science, National Taiwan University, Taipei, Taiwan – sequence: 2 givenname: Der-Yen surname: Lee fullname: Lee, Der-Yen organization: Technology Commons, College of Life Science, National Taiwan University, Taipei, Taiwan – sequence: 3 givenname: Hao-Ching surname: Wang fullname: Wang, Hao-Ching organization: Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan – sequence: 4 givenname: Shih-Ting surname: Kang fullname: Kang, Shih-Ting organization: Institute of Bioinformatics and Biosignal Transduction, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan Department of Life Science, College of Life Science, National Taiwan University, Taipei, Taiwan – sequence: 5 givenname: Pung-Pung surname: Hwang fullname: Hwang, Pung-Pung organization: Institute of Cellular and Organismic Biology, Academia Sinica, Taipei, Taiwan – sequence: 6 givenname: Guang-Hsiung surname: Kou fullname: Kou, Guang-Hsiung organization: Department of Life Science, College of Life Science, National Taiwan University, Taipei, Taiwan – sequence: 7 givenname: Ming-Fen surname: Huang fullname: Huang, Ming-Fen organization: Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan – sequence: 8 givenname: Geen-Dong surname: Chang fullname: Chang, Geen-Dong email: gdchang@ntu.edu.tw, gracelow@mail.ncku.edu.tw organization: Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan gdchang@ntu.edu.tw gracelow@mail.ncku.edu.tw – sequence: 9 givenname: Chu-Fang surname: Lo fullname: Lo, Chu-Fang email: gdchang@ntu.edu.tw, gracelow@mail.ncku.edu.tw organization: Institute of Bioinformatics and Biosignal Transduction, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan Department of Life Science, College of Life Science, National Taiwan University, Taipei, Taiwan gdchang@ntu.edu.tw gracelow@mail.ncku.edu.tw |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25378496$$D View this record in MEDLINE/PubMed |
BookMark | eNqNkU1v1DAQhi1URLcLN87INziQ4rEdJ7kgoQpKUSUufN0sxxk3hsRebG_R_gL-drPdUsGNk6XxM69m5jkhRyEGJOQpsFMA3r768OXilHEBbQXyAVkB69qqrkEekRVjnFe1aL8dk5OcvzMGUir5iBzzWjSt7NSK_P46-oI0b2KheReGFGek1z5tM92kWNAH-sMHk5ECHdChKZmWEekYc6EWp-l5pj7FUP3yZRzjNPhwdQuGpWVGO5rg80z7HfWhYDK27IE9fIhwmJJfao_JQ2emjE_u3jX5_O7tp7P31eXH84uzN5eVlYqVSrKuc8IwNgxWWFk70XIOvOet7azremXsIBlXQkkF0DtQXMjGgVN9DUK1Yk1eH3I3237GwWIoyUx6k_xs0k5H4_W_P8GP-ipeaykYU7xZAl7cBaT4c4u56Nnn_SFMwLjNGlQtVSdFo_4DlVyxplvsrcnLA2pTzDmhu58ImN5r1otmfatZg1zwZ39vcQ__8SpuALD_p1w |
CitedBy_id | crossref_primary_10_1016_j_fsi_2018_05_030 crossref_primary_10_1016_j_dci_2018_01_008 crossref_primary_10_1007_s10499_022_01009_z crossref_primary_10_3389_fimmu_2021_697397 crossref_primary_10_3390_ijms20235857 crossref_primary_10_3389_fmicb_2021_796049 crossref_primary_10_3390_biom10060825 crossref_primary_10_1016_j_dci_2020_103667 crossref_primary_10_1016_j_dci_2020_103810 crossref_primary_10_1016_j_fsi_2018_12_022 crossref_primary_10_1128_JVI_02261_16 crossref_primary_10_1016_j_freeradbiomed_2021_01_026 crossref_primary_10_1016_j_fsi_2018_10_007 crossref_primary_10_1096_fj_202100726RR crossref_primary_10_3390_ijms18102126 crossref_primary_10_3390_v8010023 crossref_primary_10_1016_j_dci_2020_103947 crossref_primary_10_1016_j_fsi_2018_12_027 crossref_primary_10_3390_ijms23126835 crossref_primary_10_1007_s11010_016_2715_0 crossref_primary_10_3390_antibiotics10070848 |
Cites_doi | 10.1006/abio.2002.5611 10.1016/j.fsi.2007.01.010 10.1128/JVI.05385-11 10.1016/j.fsi.2005.12.003 10.1023/A:1008127709325 10.1371/journal.ppat.1003935 10.1128/MCB.15.9.5152 10.1006/viro.2001.1002 10.1016/j.mam.2005.07.013 10.1146/annurev.bi.54.070185.005055 10.5483/BMBRep.2008.41.9.670 10.1099/jmm.0.46199-0 10.3201/eid0503.990305 10.1016/j.molcel.2006.07.019 10.1042/bj3200129 10.1074/jbc.M310022200 10.1006/viro.2001.1091 10.1016/0304-4165(81)90255-5 10.1038/nsmb1288 10.1002/prot.24251 10.1042/bj2610787 10.1182/blood.V94.10.3593.422k26_3593_3603 10.1146/annurev.nutr.20.1.627 10.1016/j.dci.2004.07.001 10.1016/0076-6879(90)86093-B 10.1182/blood-2002-07-2158 10.1146/annurev.bi.56.070187.001445 10.1111/j.1365-2958.2004.04169.x 10.1073/pnas.97.6.2474 10.1016/S0021-9258(19)37165-0 10.1128/JVI.75.21.10557-10562.2001 10.1016/j.dci.2007.05.005 10.1073/pnas.84.19.6730 10.1016/j.gene.2004.04.027 10.1073/pnas.84.23.8478 10.3233/JAD-2008-13409 10.1042/CS20040278 10.1016/j.fsi.2006.10.012 10.1146/annurev.biochem.67.1.71 10.1074/jbc.272.33.20736 10.1016/S0021-9258(17)43653-2 10.1016/j.jbiotec.2006.03.010 10.1074/mcp.M113.029199 10.1016/j.fsi.2009.12.013 10.1152/ajpcell.1995.268.6.C1354 10.1006/viro.1994.1636 10.1074/jbc.271.34.20291 10.1074/jbc.M010806200 |
ContentType | Journal Article |
Copyright | Copyright © 2015, American Society for Microbiology. All Rights Reserved. Copyright © 2015, American Society for Microbiology. All Rights Reserved. 2015 American Society for Microbiology |
Copyright_xml | – notice: Copyright © 2015, American Society for Microbiology. All Rights Reserved. – notice: Copyright © 2015, American Society for Microbiology. All Rights Reserved. 2015 American Society for Microbiology |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 7U9 H94 5PM |
DOI | 10.1128/JVI.02318-14 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic Virology and AIDS Abstracts AIDS and Cancer Research Abstracts PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic AIDS and Cancer Research Abstracts Virology and AIDS Abstracts |
DatabaseTitleList | MEDLINE CrossRef MEDLINE - Academic AIDS and Cancer Research Abstracts |
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 | fulltext_linktorsrc |
Discipline | Biology |
DocumentTitleAlternate | PK1, Ferritin, and Iron-Withholding Mechanism |
EISSN | 1098-5514 |
Editor | McFadden, G. |
Editor_xml | – sequence: 1 givenname: G. surname: McFadden fullname: McFadden, G. |
EndPage | 1093 |
ExternalDocumentID | 10_1128_JVI_02318_14 25378496 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- -~X 0R~ 18M 29L 2WC 39C 4.4 53G 5GY 5RE 5VS 85S ABPPZ ACGFO ACNCT ADBBV AENEX AGVNZ ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BTFSW CGR CS3 CUY CVF DIK E3Z EBS ECM EIF EJD F5P FRP GX1 H13 HYE HZ~ IH2 KQ8 N9A NPM O9- OK1 P2P RHF RHI RNS RPM RSF TR2 UCJ UPT W2D W8F WH7 WOQ YQT ~02 ~KM AAYXX CITATION 7X8 7U9 H94 5PM |
ID | FETCH-LOGICAL-c460t-4099f3a00ddc3c45f382212b28c9cf9b6acd4026364611bf162347f1f6b513683 |
IEDL.DBID | RPM |
ISSN | 0022-538X |
IngestDate | Tue Sep 17 21:27:01 EDT 2024 Sat Aug 17 00:30:33 EDT 2024 Sat Aug 17 03:46:31 EDT 2024 Thu Sep 12 17:16:36 EDT 2024 Sat Sep 28 08:03:10 EDT 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 2 |
Language | English |
License | Copyright © 2015, American Society for Microbiology. All Rights Reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c460t-4099f3a00ddc3c45f382212b28c9cf9b6acd4026364611bf162347f1f6b513683 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Citation Lin S-J, Lee D-Y, Wang H-C, Kang S-T, Hwang P-P, Kou G-H, Huang M-F, Chang G-D, Lo C-F. 2015. White spot syndrome virus protein kinase 1 defeats the host cell's iron-withholding defense mechanism by interacting with host ferritin. J Virol 89:1083–1093. doi:10.1128/JVI.02318-14. S.-J.L. and D.-Y.L. contributed equally to this article. |
OpenAccessLink | https://jvi.asm.org/content/jvi/89/2/1083.full.pdf |
PMID | 25378496 |
PQID | 1642607902 |
PQPubID | 23479 |
PageCount | 11 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_4300627 proquest_miscellaneous_1654694376 proquest_miscellaneous_1642607902 crossref_primary_10_1128_JVI_02318_14 pubmed_primary_25378496 |
PublicationCentury | 2000 |
PublicationDate | 2015-Jan-15 |
PublicationDateYYYYMMDD | 2015-01-15 |
PublicationDate_xml | – month: 01 year: 2015 text: 2015-Jan-15 day: 15 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: 1752 N St., N.W., Washington, DC |
PublicationTitle | Journal of virology |
PublicationTitleAlternate | J Virol |
PublicationYear | 2015 |
Publisher | American Society for Microbiology |
Publisher_xml | – name: American Society for Microbiology |
References | 3479802 - Proc Natl Acad Sci U S A. 1987 Dec;84(23):8478-82 9252395 - J Biol Chem. 1997 Aug 15;272(33):20736-41 7975217 - Virology. 1994 Nov 15;205(1):210-6 14573596 - J Biol Chem. 2004 Jan 9;279(2):1491-8 3304136 - Annu Rev Biochem. 1987;56:289-315 11581431 - J Virol. 2001 Nov;75(21):10557-62 12456502 - Blood. 2003 Apr 1;101(7):2858-64 17628672 - Dev Comp Immunol. 2008;32(2):121-33 17337210 - Fish Shellfish Immunol. 2007 Aug;23(2):459-72 11448154 - Virology. 2001 Jul 20;286(1):7-22 6271255 - Biochim Biophys Acta. 1981 Nov 5;677(3-4):417-23 10552971 - Blood. 1999 Nov 15;94(10):3593-603 2172697 - Methods Enzymol. 1990;186:1-85 23344859 - Proteins. 2013 Jun;81(6):1042-50 11969183 - Anal Biochem. 2002 May 1;304(1):1-18 2803243 - Biochem J. 1989 Aug 1;261(3):787-92 10716984 - Proc Natl Acad Sci U S A. 2000 Mar 14;97(6):2474-9 3477805 - Proc Natl Acad Sci U S A. 1987 Oct;84(19):6730-4 8947477 - Biochem J. 1996 Nov 15;320 ( Pt 1):129-35 15450750 - Dev Comp Immunol. 2005;29(2):103-12 7651432 - Mol Cell Biol. 1995 Sep;15(9):5152-64 15877545 - Clin Sci (Lond). 2005 Sep;109(3):277-86 11301321 - J Biol Chem. 2001 Jun 29;276(26):24301-8 16973432 - Mol Cell. 2006 Sep 15;23(6):801-8 17704817 - Nat Struct Mol Biol. 2007 Sep;14(9):875-7 7611353 - Am J Physiol. 1995 Jun;268(6 Pt 1):C1354-61 21976644 - J Virol. 2011 Dec;85(24):12919-28 16687582 - J Med Microbiol. 2006 Jun;55(Pt 6):661-8 8702762 - J Biol Chem. 1996 Aug 23;271(34):20291-9 24550730 - PLoS Pathog. 2014 Feb;10(2):e1003935 6608521 - J Biol Chem. 1984 Jan 10;259(1):278-83 24217020 - Mol Cell Proteomics. 2014 Jan;13(1):269-82 10940348 - Annu Rev Nutr. 2000;20:627-62 9759483 - Annu Rev Biochem. 1998;67:71-98 1517245 - J Biol Chem. 1992 Sep 5;267(25):18148-53 16621097 - J Biotechnol. 2006 Sep 1;125(2):173-84 20045064 - Fish Shellfish Immunol. 2010 Apr;28(4):542-8 15255894 - Mol Microbiol. 2004 Aug;53(3):807-20 16546402 - Fish Shellfish Immunol. 2006 Sep;21(3):279-83 15315822 - Gene. 2004 Sep 1;338(2):187-95 16125765 - Mol Aspects Med. 2005 Aug-Oct;26(4-5):235-44 18487852 - J Alzheimers Dis. 2008 May;13(4):451-63 2862839 - Annu Rev Biochem. 1985;54:1015-69 17175172 - Fish Shellfish Immunol. 2007 Jul;23(1):242-6 11324757 - Virus Genes. 2001 Mar;22(2):201-7 18823592 - BMB Rep. 2008 Sep 30;41(9):670-7 11689058 - Virology. 2001 Oct 25;289(2):362-77 10341171 - Emerg Infect Dis. 1999 May-Jun;5(3):346-52 e_1_3_2_26_2 e_1_3_2_49_2 e_1_3_2_28_2 e_1_3_2_41_2 e_1_3_2_20_2 e_1_3_2_43_2 e_1_3_2_22_2 e_1_3_2_45_2 e_1_3_2_24_2 e_1_3_2_47_2 e_1_3_2_9_2 e_1_3_2_16_2 e_1_3_2_37_2 e_1_3_2_7_2 e_1_3_2_18_2 e_1_3_2_39_2 e_1_3_2_10_2 e_1_3_2_31_2 e_1_3_2_5_2 e_1_3_2_12_2 e_1_3_2_33_2 e_1_3_2_3_2 e_1_3_2_14_2 e_1_3_2_35_2 e_1_3_2_50_2 e_1_3_2_27_2 e_1_3_2_48_2 e_1_3_2_29_2 e_1_3_2_40_2 e_1_3_2_21_2 e_1_3_2_42_2 e_1_3_2_23_2 e_1_3_2_44_2 e_1_3_2_25_2 e_1_3_2_46_2 e_1_3_2_15_2 e_1_3_2_38_2 e_1_3_2_8_2 e_1_3_2_17_2 e_1_3_2_6_2 e_1_3_2_19_2 e_1_3_2_30_2 e_1_3_2_32_2 e_1_3_2_11_2 e_1_3_2_34_2 e_1_3_2_4_2 e_1_3_2_13_2 e_1_3_2_36_2 e_1_3_2_2_2 |
References_xml | – ident: e_1_3_2_26_2 doi: 10.1006/abio.2002.5611 – ident: e_1_3_2_16_2 doi: 10.1016/j.fsi.2007.01.010 – ident: e_1_3_2_28_2 doi: 10.1128/JVI.05385-11 – ident: e_1_3_2_23_2 doi: 10.1016/j.fsi.2005.12.003 – ident: e_1_3_2_20_2 doi: 10.1023/A:1008127709325 – ident: e_1_3_2_7_2 doi: 10.1371/journal.ppat.1003935 – ident: e_1_3_2_48_2 – ident: e_1_3_2_12_2 doi: 10.1128/MCB.15.9.5152 – ident: e_1_3_2_21_2 doi: 10.1006/viro.2001.1002 – ident: e_1_3_2_32_2 doi: 10.1016/j.mam.2005.07.013 – ident: e_1_3_2_33_2 doi: 10.1146/annurev.bi.54.070185.005055 – ident: e_1_3_2_17_2 doi: 10.5483/BMBRep.2008.41.9.670 – ident: e_1_3_2_9_2 doi: 10.1099/jmm.0.46199-0 – ident: e_1_3_2_8_2 doi: 10.3201/eid0503.990305 – ident: e_1_3_2_36_2 doi: 10.1016/j.molcel.2006.07.019 – ident: e_1_3_2_39_2 doi: 10.1042/bj3200129 – ident: e_1_3_2_35_2 doi: 10.1074/jbc.M310022200 – ident: e_1_3_2_19_2 doi: 10.1006/viro.2001.1091 – ident: e_1_3_2_50_2 doi: 10.1016/0304-4165(81)90255-5 – ident: e_1_3_2_37_2 doi: 10.1038/nsmb1288 – ident: e_1_3_2_43_2 doi: 10.1002/prot.24251 – ident: e_1_3_2_49_2 doi: 10.1042/bj2610787 – ident: e_1_3_2_3_2 doi: 10.1182/blood.V94.10.3593.422k26_3593_3603 – ident: e_1_3_2_31_2 doi: 10.1146/annurev.nutr.20.1.627 – ident: e_1_3_2_14_2 doi: 10.1016/j.dci.2004.07.001 – ident: e_1_3_2_46_2 doi: 10.1016/0076-6879(90)86093-B – ident: e_1_3_2_11_2 doi: 10.1182/blood-2002-07-2158 – ident: e_1_3_2_4_2 doi: 10.1146/annurev.bi.56.070187.001445 – ident: e_1_3_2_6_2 doi: 10.1111/j.1365-2958.2004.04169.x – ident: e_1_3_2_40_2 doi: 10.1073/pnas.97.6.2474 – ident: e_1_3_2_2_2 doi: 10.1016/S0021-9258(19)37165-0 – ident: e_1_3_2_10_2 doi: 10.1128/JVI.75.21.10557-10562.2001 – ident: e_1_3_2_25_2 doi: 10.1016/j.dci.2007.05.005 – ident: e_1_3_2_30_2 doi: 10.1073/pnas.84.19.6730 – ident: e_1_3_2_44_2 doi: 10.1016/j.gene.2004.04.027 – ident: e_1_3_2_29_2 doi: 10.1073/pnas.84.23.8478 – ident: e_1_3_2_5_2 doi: 10.3233/JAD-2008-13409 – ident: e_1_3_2_45_2 doi: 10.1042/CS20040278 – ident: e_1_3_2_22_2 doi: 10.1016/j.fsi.2006.10.012 – ident: e_1_3_2_34_2 doi: 10.1146/annurev.biochem.67.1.71 – ident: e_1_3_2_13_2 doi: 10.1074/jbc.272.33.20736 – ident: e_1_3_2_47_2 doi: 10.1016/S0021-9258(17)43653-2 – ident: e_1_3_2_15_2 doi: 10.1016/j.jbiotec.2006.03.010 – ident: e_1_3_2_24_2 doi: 10.1074/mcp.M113.029199 – ident: e_1_3_2_18_2 doi: 10.1016/j.fsi.2009.12.013 – ident: e_1_3_2_27_2 doi: 10.1152/ajpcell.1995.268.6.C1354 – ident: e_1_3_2_41_2 doi: 10.1006/viro.1994.1636 – ident: e_1_3_2_38_2 doi: 10.1074/jbc.271.34.20291 – ident: e_1_3_2_42_2 doi: 10.1074/jbc.M010806200 |
SSID | ssj0014464 |
Score | 2.3188853 |
Snippet | Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels in a cell,... ABSTRACT Iron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels... UNLABELLEDIron is an essential nutrient for nearly all living organisms, including both hosts and invaders. Proteins such as ferritin regulate the iron levels... |
SourceID | pubmedcentral proquest crossref pubmed |
SourceType | Open Access Repository Aggregation Database Index Database |
StartPage | 1083 |
SubjectTerms | Animals Cell Line Centrifugation Defense Mechanisms Ferritins - metabolism Host-Pathogen Interactions Iron - metabolism Protein Binding Protein Interaction Mapping Protein Kinases - metabolism Quartz Crystal Microbalance Techniques Two-Hybrid System Techniques Viral Proteins - metabolism Virus-Cell Interactions White spot syndrome virus White spot syndrome virus 1 - physiology |
Title | White spot syndrome virus protein kinase 1 defeats the host cell's iron-withholding defense mechanism by interacting with host ferritin |
URI | https://www.ncbi.nlm.nih.gov/pubmed/25378496 https://search.proquest.com/docview/1642607902 https://search.proquest.com/docview/1654694376 https://pubmed.ncbi.nlm.nih.gov/PMC4300627 |
Volume | 89 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9wwEB6SQKGX0nc3faBCS0_etayXfSzbLpuULYE06d6MpbWIYVde1t5DfkH-dkayHZIWeujVHsnGM9bMJ818A_AJYxC1komJFNpTxLVRUcGVjlJ0D6nQBdWh2cTip5xf8NOlWB6AGGphQtK-0dXYrTdjV12F3MrtxkyGPLHJ2WLKmS_9U5NDOFSMDRC9PzpAfMMHinD8m5dDtnuSTk4vT8ae7wxxk-_HkwimUu7p-u-7pL_izD_TJe_5n9lTeNIHjuRr94LP4KB0z-FR10ry-gXchE535Hxbt-S8ZyEgl9Vu35AzT8VQOfKjcuiyCCXfSosrcEMw9iPzumnJtFyvvzTkZFe76HfVXvVHUkHQ4ZBF6euDq2ZD9DUJe4i-HAIF_C5uN8XMMzzitZdwMfv-azqP-iYLkeEybhE_ZpllRRyvVoYZLizDkIEmOklNZmymZWFWiDElk1xSqi3FeIkrS63UgjKZsldw5GpXvgGSFTiRZDrOUsut4EXp2eYRuktbGNTXCD4P3znfdlwaecAgSZqjavKgGsQiI_g4KCFHY_cnGIUr632TI7ZD_KWyOPmXjEDIz3HhHMHrTnF3Txs0PgL1QKV3Ap5s--EdtMFAut3b3PF_j3wLjzHY8pmSERXv4Kjd7cv3GNC0-kMw4Ft0j_Ua |
link.rule.ids | 230,315,733,786,790,891,27955,27956,53825,53827 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3JbtswEB2kKYr2knRL66YLC7ToSbIWkpKOgVvDTuIgQBLXN0GkRUSoTRmWfEh-oL-dISUFSQoUaK_iomWGmnnkzBuAL-iDRHMeSCdCfXKokJGT0Ug4MZqHmInMF7bYxOSEjy7o4YzNtoB1uTA2aF-KwtWLpauLSxtbuVrKfhcn1j-dDGhoUv-i_iN4jOs1YB1Ibw8PEOHQjiQc22ddvHsQ9w-nY9cwniFyMhV5AhZGMTWE_XeN0h-e5sOAyTsWaLgL0-7Zm8CTX-6mFq68fkDr-M8v9xx2Wp-UHDTNL2Ar1y_hSVOl8uoV_LZF9MjZqqzJWUtwQKbFelORU8PyUGhyVGi0hsQn33OFP_eKoFtJRmVVk0G-WHyryHhdaudnUV-2p122o8Yhk9ykHhfVkogrYrcnTaYFdjAbxM0UQ0Meiddew8Xwx_lg5LT1GxxJuVcjNE0SFWaeN5_LUFKmUFZoKUUQy0SqRPBMzhG-8pBT7vtC-eiK0Uj5igvmhzwO92Bblzp_CyTJcCIeCi-JFVWMZrkhss9FwFUm8Wv14GsnwHTV0HSkFt4EcYoyT63MEeb04HMn3RTXkTkcyXRebqoUYSNCuyjxgr_1YZQnFP_JPXjTaMTt3TpV6kF0T1duOxge7_stqAGWz7uV-Lv_HvkJno7OJ8fp8fjkaB-eoU9nAjIdn72H7Xq9yT-g31SLj3aV3AAGkRcV |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELagCMSl5d2lBYwE4pS3YyfHastqt2WrlUrLiksUO7YaseusNtlD-QP8bcZOUm2LxKHXeOw8ZpyZzx5_g9AniEFYQUPhMLAnh3DBnJww7iTgHpKY5wG3xSamZ3R8QU7m8Xyr1JdN2he8dPVi6eryyuZWrpbC6_PEvNl0SCJz9I95q0J5D9EjmLMh64F6t4EAKIf0ROHQPu9z3sPEO7mcuIb1DNCTqcoTxhFLiCHt33ZM_0Sbd5Mmt7zQaA_97J-_TT755W4a7orfd6gd7_WCz9BuF5vio1bkOXog9Qv0uK1Wef0S_bHF9PD5qmrweUd0gC_L9abGM8P2UGp8WmrwijjAx1LBT77GEF7icVU3eCgXiy81nqwr7fwom6tu18sKaugyleYIclkvMb_GdpnSnLgAAbNQ3A4xMiSScO0Vuhh9_T4cO10dB0cQ6jcAUdNURbnvF4WIBIkV6As8Jg8TkQqVcpqLAmAsjSihQcBVACEZYSpQlMdBRJPoNdrRlZb7CKc5DEQj7qeJIiomuTSE9pKHVOUCvtgAfe6VmK1auo7MwpwwyUDvmdU7wJ0B-thrOIP5ZDZJci2rTZ0BfASIx1I__J9MTGhK4N88QG9aq7i5W29OA8Ru2cuNgOHzvt0CVmB5vTutv713zw_oyex4lH2bnJ0eoKcQ2pm8TCeID9FOs97IdxA-Nfy9nSh_AcJZGZU |
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=White+spot+syndrome+virus+protein+kinase+1+defeats+the+host+cell%27s+iron-withholding+defense+mechanism+by+interacting+with+host+ferritin&rft.jtitle=Journal+of+virology&rft.au=Lin%2C+Shin-Jen&rft.au=Lee%2C+Der-Yen&rft.au=Wang%2C+Hao-Ching&rft.au=Kang%2C+Shih-Ting&rft.date=2015-01-15&rft.eissn=1098-5514&rft.volume=89&rft.issue=2&rft.spage=1083&rft_id=info:doi/10.1128%2FJVI.02318-14&rft_id=info%3Apmid%2F25378496&rft.externalDocID=25378496 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-538X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-538X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-538X&client=summon |