APOBEC3G cytidine deaminase association with coronavirus nucleocapsid protein.
Identifieur interne : 001952 ( PubMed/Checkpoint ); précédent : 001951; suivant : 001953APOBEC3G cytidine deaminase association with coronavirus nucleocapsid protein.
Auteurs : Shui-Mei Wang [Taïwan] ; Chin-Tien WangSource :
- Virology [ 1096-0341 ] ; 2009.
Descripteurs français
- KwdFr :
- APOBEC-3G Deaminase, Cartographie peptidique, Cytidine deaminase (métabolisme), Humains, Liaison aux protéines, Lignée cellulaire, Protéine de capside p24 du VIH (métabolisme), Protéines de fusion recombinantes, Protéines nucléocapside (métabolisme), Régulation de l'expression des gènes viraux (physiologie), Virus du SRAS (métabolisme).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cytidine Deaminase, HIV Core Protein p24, Nucleocapsid Proteins.
- chemical : APOBEC-3G Deaminase, Recombinant Fusion Proteins.
- metabolism : SARS Virus.
- physiology : Gene Expression Regulation, Viral.
- Cell Line, Humans, Peptide Mapping, Protein Binding.
Abstract
We previously reported that replacing HIV-1 nucleocapsid (NC) domain with SARS-CoV nucleocapsid (N) residues 2-213, 215-421, or 234-421 results in efficient virus-like particle (VLP) production at a level comparable to that of wild-type HIV-1. In this study we demonstrate that these chimeras are capable of packaging large amounts of human APOBEC3G (hA3G), and that an HIV-1 Gag chimera containing the carboxyl-terminal half of human coronavirus 229E (HCoV-229E) N as a substitute for NC is capable of directing VLP assembly and efficiently packaging hA3G. When co-expressed with SARS-CoV N and M (membrane) proteins, hA3G was efficiently incorporated into SARS-CoV VLPs. Data from GST pull-down assays suggest that the N sequence involved in N-hA3G interactions is located between residues 86 and 302. Like HIV-1 NC, the SARS-CoV or HCoV-229E N-associated with hA3G depends on the presence of RNA, with the first linker region essential for hA3G packaging into both HIV-1 and SARS-CoV VLPs. The results raise the possibility that hA3G is capable of associating with different species of viral structural proteins through a potentially common, RNA-mediated mechanism.
DOI: 10.1016/j.virol.2009.03.010
PubMed: 19345973
Affiliations:
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Medical Research and Education, Taipei Veterans General Hospital, Taipei</wicri:regionArea><wicri:noRegion>Taipei</wicri:noRegion></affiliation></author><author><name sortKey="Wang, Chin Tien" sort="Wang, Chin Tien" uniqKey="Wang C" first="Chin-Tien" last="Wang">Chin-Tien Wang</name></author></analytic><series><title level="j">Virology</title><idno type="eISSN">1096-0341</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>APOBEC-3G Deaminase</term><term>Cell Line</term><term>Cytidine Deaminase (metabolism)</term><term>Gene Expression Regulation, Viral (physiology)</term><term>HIV Core Protein p24 (metabolism)</term><term>Humans</term><term>Nucleocapsid Proteins (metabolism)</term><term>Peptide Mapping</term><term>Protein Binding</term><term>Recombinant Fusion Proteins</term><term>SARS Virus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>APOBEC-3G Deaminase</term><term>Cartographie peptidique</term><term>Cytidine deaminase (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéine de capside p24 du VIH (métabolisme)</term><term>Protéines de fusion recombinantes</term><term>Protéines nucléocapside (métabolisme)</term><term>Régulation de l'expression des gènes viraux (physiologie)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytidine Deaminase</term><term>HIV Core Protein p24</term><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>APOBEC-3G Deaminase</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytidine deaminase</term><term>Protéine de capside p24 du VIH</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Régulation de l'expression des gènes viraux</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Peptide Mapping</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>APOBEC-3G Deaminase</term><term>Cartographie peptidique</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines de fusion recombinantes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We previously reported that replacing HIV-1 nucleocapsid (NC) domain with SARS-CoV nucleocapsid (N) residues 2-213, 215-421, or 234-421 results in efficient virus-like particle (VLP) production at a level comparable to that of wild-type HIV-1. In this study we demonstrate that these chimeras are capable of packaging large amounts of human APOBEC3G (hA3G), and that an HIV-1 Gag chimera containing the carboxyl-terminal half of human coronavirus 229E (HCoV-229E) N as a substitute for NC is capable of directing VLP assembly and efficiently packaging hA3G. When co-expressed with SARS-CoV N and M (membrane) proteins, hA3G was efficiently incorporated into SARS-CoV VLPs. Data from GST pull-down assays suggest that the N sequence involved in N-hA3G interactions is located between residues 86 and 302. Like HIV-1 NC, the SARS-CoV or HCoV-229E N-associated with hA3G depends on the presence of RNA, with the first linker region essential for hA3G packaging into both HIV-1 and SARS-CoV VLPs. The results raise the possibility that hA3G is capable of associating with different species of viral structural proteins through a potentially common, RNA-mediated mechanism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19345973</PMID><DateCompleted><Year>2009</Year><Month>05</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0341</ISSN><JournalIssue CitedMedium="Internet"><Volume>388</Volume><Issue>1</Issue><PubDate><Year>2009</Year><Month>May</Month><Day>25</Day></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>APOBEC3G cytidine deaminase association with coronavirus nucleocapsid protein.</ArticleTitle><Pagination><MedlinePgn>112-20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virol.2009.03.010</ELocationID><Abstract><AbstractText>We previously reported that replacing HIV-1 nucleocapsid (NC) domain with SARS-CoV nucleocapsid (N) residues 2-213, 215-421, or 234-421 results in efficient virus-like particle (VLP) production at a level comparable to that of wild-type HIV-1. In this study we demonstrate that these chimeras are capable of packaging large amounts of human APOBEC3G (hA3G), and that an HIV-1 Gag chimera containing the carboxyl-terminal half of human coronavirus 229E (HCoV-229E) N as a substitute for NC is capable of directing VLP assembly and efficiently packaging hA3G. When co-expressed with SARS-CoV N and M (membrane) proteins, hA3G was efficiently incorporated into SARS-CoV VLPs. Data from GST pull-down assays suggest that the N sequence involved in N-hA3G interactions is located between residues 86 and 302. Like HIV-1 NC, the SARS-CoV or HCoV-229E N-associated with hA3G depends on the presence of RNA, with the first linker region essential for hA3G packaging into both HIV-1 and SARS-CoV VLPs. The results raise the possibility that hA3G is capable of associating with different species of viral structural proteins through a potentially common, RNA-mediated mechanism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Shui-Mei</ForeName><Initials>SM</Initials><AffiliationInfo><Affiliation>Department of Medical Research and Education, Taipei Veterans General Hospital, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Chin-Tien</ForeName><Initials>CT</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>04</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United 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|type= RBID
|clé= pubmed:19345973
|texte= APOBEC3G cytidine deaminase association with coronavirus nucleocapsid protein.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i -Sk "pubmed:19345973" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |