HuR binding to AU-rich elements present in the 3' untranslated region of Classical swine fever virus
Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of th...
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Published in | Virology journal Vol. 8; no. 1; p. 340 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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BioMed Central Ltd
06.07.2011
BioMed Central BMC |
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ISSN | 1743-422X 1743-422X |
DOI | 10.1186/1743-422X-8-340 |
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Abstract | Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV.
Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence.
This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region. |
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AbstractList | Abstract Background Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV. Results Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence. Conclusions This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region. Background Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV. Results Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence. Conclusions This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region. Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV. Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence. This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region. Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV. Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence. This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region. Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV.BACKGROUNDClassical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV.Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence.RESULTSUsing RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence.This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region.CONCLUSIONSThis study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region. |
ArticleNumber | 340 |
Audience | Academic |
Author | Chan, Meng-Yu Tsai, Ching-Hsiu Nadar, Muthukumar Tseng, Joseph T Huang, Shi-Wei Huang, Chin-Cheng |
AuthorAffiliation | 1 Graduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan 3 Institute of Bioinformatics, National Cheng Kung University, Tainan 701, Taiwan 2 Department of Hog Cholera, Animal Health Research Institute, Council of Agriculture, Taipei, Taiwan |
AuthorAffiliation_xml | – name: 3 Institute of Bioinformatics, National Cheng Kung University, Tainan 701, Taiwan – name: 2 Department of Hog Cholera, Animal Health Research Institute, Council of Agriculture, Taipei, Taiwan – name: 1 Graduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan |
Author_xml | – sequence: 1 givenname: Muthukumar surname: Nadar fullname: Nadar, Muthukumar – sequence: 2 givenname: Meng-Yu surname: Chan fullname: Chan, Meng-Yu – sequence: 3 givenname: Shi-Wei surname: Huang fullname: Huang, Shi-Wei – sequence: 4 givenname: Chin-Cheng surname: Huang fullname: Huang, Chin-Cheng – sequence: 5 givenname: Joseph T surname: Tseng fullname: Tseng, Joseph T – sequence: 6 givenname: Ching-Hsiu surname: Tsai fullname: Tsai, Ching-Hsiu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21729330$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1128/JVI.76.12.6114-6120.2002 10.1128/JVI.77.15.8181-8186.2003 10.1093/emboj/cdf513 10.1023/B:MBIL.0000023747.76845.13 10.1101/gad.248902 10.1128/JVI.72.11.8789-8796.1998 10.1093/nar/gki1012 10.1128/MCB.24.10.4522-4533.2004 10.1128/MCB.21.3.721-730.2001 10.1073/pnas.1432104100 10.1042/BJ20070311 10.1038/nchembio.2007.14 10.1093/emboj/19.15.4154 10.1354/vp.42-4-477 10.1023/A:1007971110065 10.1242/jcs.111.21.3145 10.1074/jbc.271.21.12179 10.1023/A:1008000231604 10.1128/MCB.19.6.4311 10.1016/S0968-0004(00)89102-1 10.1091/mbc.E07-09-0962 10.1073/pnas.97.7.3073 10.1093/nar/gkl1061 10.1128/jvi.69.5.2932-2945.1995 10.1128/JVI.76.23.11989-12000.2002 10.1083/jcb.200205044 10.1006/prep.1995.1004 10.1017/S1355838200000662 10.1038/nature04078 10.1093/emboj/17.12.3461 10.4161/cc.7.20.6884 |
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References | JL Dean (1441_CR25) 2001; 21 M Gale Jr. (1441_CR5) 2005; 436 U Atasoy (1441_CR26) 1998; 111 M Xiao (1441_CR8) 2004; 38 C Barreau (1441_CR23) 2005; 33 JW Lin (1441_CR6) 2007; 35 SS Peng (1441_CR17) 1998; 17 M Kullmann (1441_CR31) 2002; 16 T Ito (1441_CR9) 1998; 72 M Piecyk (1441_CR18) 2000; 19 W Tan (1441_CR11) 1995; 69 NC Meisner (1441_CR32) 2007; 3 JO Langland (1441_CR24) 1995; 6 W Li (1441_CR14) 2002; 76 HH Kim (1441_CR30) 2008; 7 HL Cook (1441_CR12) 2004; 24 JH Cheng (1441_CR7) 2002; 76 CT DeMaria (1441_CR15) 1996; 271 IE Gallouzi (1441_CR28) 2000; 97 SM Abmayr (1441_CR22) 2006; Chapter 12 CH Yeh (1441_CR19) 2008; 19 F Iseni (1441_CR13) 2002; 21 S Bandyopadhyay (1441_CR27) 2008; 410 PJ Sanchez-Cordon (1441_CR1) 2005; 42 S Vilcek (1441_CR20) 1997; 15 CY Chen (1441_CR10) 1995; 20 K Mazan-Mamczarz (1441_CR29) 2003; 100 S Vilcek (1441_CR21) 1999; 18 VG Kolupaeva (1441_CR2) 2000; 6 M Bushell (1441_CR4) 2002; 158 P Ahlquist (1441_CR3) 2003; 77 WS Lai (1441_CR16) 1999; 19 17632515 - Nat Chem Biol. 2007 Aug;3(8):508-15 16107833 - Nature. 2005 Aug 18;436(7053):939-45 18265374 - Curr Protoc Mol Biol. 2006 Aug;Chapter 12:Unit 12.1 9628881 - EMBO J. 1998 Jun 15;17(12):3461-70 12464637 - Genes Dev. 2002 Dec 1;16(23):3087-99 11154260 - Mol Cell Biol. 2001 Feb;21(3):721-30 8647811 - J Biol Chem. 1996 May 24;271(21):12179-84 10330172 - Mol Cell Biol. 1999 Jun;19(6):4311-23 11142379 - RNA. 2000 Dec;6(12):1791-807 10921895 - EMBO J. 2000 Aug 1;19(15):4154-63 12414941 - J Virol. 2002 Dec;76(23):11989-2000 15125241 - Mol Biol (Mosk). 2004 Mar-Apr;38(2):343-51 17924856 - Biochem J. 2008 Feb 15;410(1):177-86 18579691 - Mol Biol Cell. 2008 Sep;19(9):3812-22 12021344 - J Virol. 2002 Jun;76(12):6114-20 12163463 - J Cell Biol. 2002 Aug 5;158(3):395-9 16391004 - Nucleic Acids Res. 2005;33(22):7138-50 10737787 - Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3073-8 16006607 - Vet Pathol. 2005 Jul;42(4):477-88 12857886 - J Virol. 2003 Aug;77(15):8181-6 9763509 - J Cell Sci. 1998 Nov;111 ( Pt 21):3145-56 9765423 - J Virol. 1998 Nov;72(11):8789-96 15121869 - Mol Cell Biol. 2004 May;24(10):4522-33 8578590 - Trends Biochem Sci. 1995 Nov;20(11):465-70 18927508 - Cell Cycle. 2008 Oct;7(20):3124-6 10403696 - Virus Genes. 1999;18(2):107-14 12821781 - Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8354-9 17169994 - Nucleic Acids Res. 2007;35(2):424-32 9421882 - Virus Genes. 1997;15(2):181-6 7538839 - Protein Expr Purif. 1995 Feb;6(1):25-32 12356730 - EMBO J. 2002 Oct 1;21(19):5141-50 7707519 - J Virol. 1995 May;69(5):2932-45 |
References_xml | – volume: 76 start-page: 6114 year: 2002 ident: 1441_CR7 publication-title: J Virol doi: 10.1128/JVI.76.12.6114-6120.2002 – volume: 77 start-page: 8181 year: 2003 ident: 1441_CR3 publication-title: J Virol doi: 10.1128/JVI.77.15.8181-8186.2003 – volume: 21 start-page: 5141 year: 2002 ident: 1441_CR13 publication-title: EMBO J doi: 10.1093/emboj/cdf513 – volume: 38 start-page: 343 year: 2004 ident: 1441_CR8 publication-title: Mol Biol doi: 10.1023/B:MBIL.0000023747.76845.13 – volume: 16 start-page: 3087 year: 2002 ident: 1441_CR31 publication-title: Genes Dev doi: 10.1101/gad.248902 – volume: 72 start-page: 8789 year: 1998 ident: 1441_CR9 publication-title: J Virol doi: 10.1128/JVI.72.11.8789-8796.1998 – volume: 33 start-page: 7138 year: 2005 ident: 1441_CR23 publication-title: Nucleic Acids Res doi: 10.1093/nar/gki1012 – volume: 24 start-page: 4522 year: 2004 ident: 1441_CR12 publication-title: Mol Cell Biol doi: 10.1128/MCB.24.10.4522-4533.2004 – volume: 21 start-page: 721 year: 2001 ident: 1441_CR25 publication-title: Mol Cell Biol doi: 10.1128/MCB.21.3.721-730.2001 – volume: 100 start-page: 8354 year: 2003 ident: 1441_CR29 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1432104100 – volume: 410 start-page: 177 year: 2008 ident: 1441_CR27 publication-title: Biochem J doi: 10.1042/BJ20070311 – volume: 3 start-page: 508 year: 2007 ident: 1441_CR32 publication-title: Nat Chem Biol doi: 10.1038/nchembio.2007.14 – volume: 19 start-page: 4154 year: 2000 ident: 1441_CR18 publication-title: EMBO J doi: 10.1093/emboj/19.15.4154 – volume: 42 start-page: 477 year: 2005 ident: 1441_CR1 publication-title: Vet Pathol doi: 10.1354/vp.42-4-477 – volume: 15 start-page: 181 year: 1997 ident: 1441_CR20 publication-title: Virus Genes doi: 10.1023/A:1007971110065 – volume: 111 start-page: 3145 year: 1998 ident: 1441_CR26 publication-title: J Cell Sci doi: 10.1242/jcs.111.21.3145 – volume: 271 start-page: 12179 year: 1996 ident: 1441_CR15 publication-title: J Biol Chem doi: 10.1074/jbc.271.21.12179 – volume: 18 start-page: 107 year: 1999 ident: 1441_CR21 publication-title: Virus Genes doi: 10.1023/A:1008000231604 – volume: 19 start-page: 4311 year: 1999 ident: 1441_CR16 publication-title: Mol Cell Biol doi: 10.1128/MCB.19.6.4311 – volume: 20 start-page: 465 year: 1995 ident: 1441_CR10 publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(00)89102-1 – volume: 19 start-page: 3812 year: 2008 ident: 1441_CR19 publication-title: Mol Biol Cell doi: 10.1091/mbc.E07-09-0962 – volume: 97 start-page: 3073 year: 2000 ident: 1441_CR28 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.97.7.3073 – volume: 35 start-page: 424 year: 2007 ident: 1441_CR6 publication-title: Nucleic Acids Res doi: 10.1093/nar/gkl1061 – volume: 69 start-page: 2932 year: 1995 ident: 1441_CR11 publication-title: J Virol doi: 10.1128/jvi.69.5.2932-2945.1995 – volume: 76 start-page: 11989 year: 2002 ident: 1441_CR14 publication-title: J Virol doi: 10.1128/JVI.76.23.11989-12000.2002 – volume: 158 start-page: 395 year: 2002 ident: 1441_CR4 publication-title: J Cell Biol doi: 10.1083/jcb.200205044 – volume: Chapter 12 start-page: Unit 12 11 year: 2006 ident: 1441_CR22 publication-title: Curr Protoc Mol Biol – volume: 6 start-page: 25 year: 1995 ident: 1441_CR24 publication-title: Protein Expr Purif doi: 10.1006/prep.1995.1004 – volume: 6 start-page: 1791 year: 2000 ident: 1441_CR2 publication-title: RNA doi: 10.1017/S1355838200000662 – volume: 436 start-page: 939 year: 2005 ident: 1441_CR5 publication-title: Nature doi: 10.1038/nature04078 – volume: 17 start-page: 3461 year: 1998 ident: 1441_CR17 publication-title: EMBO J doi: 10.1093/emboj/17.12.3461 – volume: 7 start-page: 3124 year: 2008 ident: 1441_CR30 publication-title: Cell Cycle doi: 10.4161/cc.7.20.6884 – reference: 17924856 - Biochem J. 2008 Feb 15;410(1):177-86 – reference: 12163463 - J Cell Biol. 2002 Aug 5;158(3):395-9 – reference: 8578590 - Trends Biochem Sci. 1995 Nov;20(11):465-70 – reference: 9765423 - J Virol. 1998 Nov;72(11):8789-96 – reference: 12821781 - Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8354-9 – reference: 12356730 - EMBO J. 2002 Oct 1;21(19):5141-50 – reference: 12857886 - J Virol. 2003 Aug;77(15):8181-6 – reference: 12464637 - Genes Dev. 2002 Dec 1;16(23):3087-99 – reference: 7707519 - J Virol. 1995 May;69(5):2932-45 – reference: 16107833 - Nature. 2005 Aug 18;436(7053):939-45 – reference: 8647811 - J Biol Chem. 1996 May 24;271(21):12179-84 – reference: 15125241 - Mol Biol (Mosk). 2004 Mar-Apr;38(2):343-51 – reference: 18927508 - Cell Cycle. 2008 Oct;7(20):3124-6 – reference: 12021344 - J Virol. 2002 Jun;76(12):6114-20 – reference: 11142379 - RNA. 2000 Dec;6(12):1791-807 – reference: 7538839 - Protein Expr Purif. 1995 Feb;6(1):25-32 – reference: 10330172 - Mol Cell Biol. 1999 Jun;19(6):4311-23 – reference: 18579691 - Mol Biol Cell. 2008 Sep;19(9):3812-22 – reference: 10737787 - Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3073-8 – reference: 18265374 - Curr Protoc Mol Biol. 2006 Aug;Chapter 12:Unit 12.1 – reference: 11154260 - Mol Cell Biol. 2001 Feb;21(3):721-30 – reference: 9628881 - EMBO J. 1998 Jun 15;17(12):3461-70 – reference: 9763509 - J Cell Sci. 1998 Nov;111 ( Pt 21):3145-56 – reference: 12414941 - J Virol. 2002 Dec;76(23):11989-2000 – reference: 10921895 - EMBO J. 2000 Aug 1;19(15):4154-63 – reference: 15121869 - Mol Cell Biol. 2004 May;24(10):4522-33 – reference: 16391004 - Nucleic Acids Res. 2005;33(22):7138-50 – reference: 17169994 - Nucleic Acids Res. 2007;35(2):424-32 – reference: 9421882 - Virus Genes. 1997;15(2):181-6 – reference: 16006607 - Vet Pathol. 2005 Jul;42(4):477-88 – reference: 10403696 - Virus Genes. 1999;18(2):107-14 – reference: 17632515 - Nat Chem Biol. 2007 Aug;3(8):508-15 |
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Snippet | Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the... Background Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV... BACKGROUND: Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV... Abstract Background Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of... |
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SubjectTerms | 3' Untranslated Regions Animals Antigens, Surface - metabolism Binding proteins Binding Sites Cell Line Classical swine fever virus Classical swine fever virus - genetics ELAV Proteins ELAV-Like Protein 1 Electrophoretic Mobility Shift Assay family Genetic aspects genus Hog cholera Host-Pathogen Interactions Physiological aspects Protein Binding Risk factors RNA RNA, Viral - genetics RNA, Viral - metabolism RNA-Binding Proteins - metabolism Swine virulence |
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Title | HuR binding to AU-rich elements present in the 3' untranslated region of Classical swine fever virus |
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