Linked Life Data

15611076

Source:http://linkedlifedata.com/resource/pubmed/id/15611076

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2005-3-7
pubmed:abstractText
The human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G), also known as CEM-15, is a host-cell factor involved in innate resistance to retroviral infection. HIV-1 viral infectivity factor (Vif) protein was shown to protect the virus from APOBEC3G-mediated viral cDNA hypermutation. The mechanism proposed for protection of the virus by HIV-1 Vif is mediated by APOBEC3G degradation through ubiquitination and the proteasomal pathway. Here we show that in Escherichia coli the APOBEC3G-induced cytidine deamination is inhibited by expression of Vif without depletion of deaminase. Moreover, inhibition of deaminase-mediated bacterial hypermutation is dependent on a single amino acid substitution D128K that renders APOBEC3G resistant to Vif inhibition. This single amino acid was elegantly proven by other authors to determine species-specific sensitivity. Our results show that in bacteria this single amino acid substitution controls Vif-dependent blocking of APOBEC3G that is dependent on a strong protein interaction. The C-terminal region of Vif is responsible for this strong protein-protein interaction. In conclusion, our experiments suggest a complement to the model of Vif-induced degradation of APOBEC3G by bringing to relevance that deaminase inhibition can also result from a direct interaction with Vif protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8765-75
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15611076-Amino Acid Sequence, pubmed-meshheading:15611076-Amino Acid Substitution, pubmed-meshheading:15611076-Apolipoproteins B, pubmed-meshheading:15611076-Binding Sites, pubmed-meshheading:15611076-Cytidine Deaminase, pubmed-meshheading:15611076-Gene Products, vif, pubmed-meshheading:15611076-HIV-1, pubmed-meshheading:15611076-Humans, pubmed-meshheading:15611076-Molecular Sequence Data, pubmed-meshheading:15611076-Mutagenesis, Site-Directed, pubmed-meshheading:15611076-Nucleoside Deaminases, pubmed-meshheading:15611076-Protein Conformation, pubmed-meshheading:15611076-Proteins, pubmed-meshheading:15611076-RNA, Messenger, pubmed-meshheading:15611076-RNA Editing, pubmed-meshheading:15611076-Repressor Proteins, pubmed-meshheading:15611076-vif Gene Products, Human Immunodeficiency Virus
pubmed:year
2005
pubmed:articleTitle
HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation.
pubmed:affiliation
Unidade de Retrovirus e Infecçôes Associadas, Centro de Patogénese Molecular, Faculdade de Farmácia, Universidade de Lisboa, Av. das Forças Armadas, 1649-019 Lisboa, Portugal.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't