Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6142318 | Virus Research | 2014 | 14 Pages |
Abstract
This review aims at briefly presenting a retrospect on the retroviral nucleocapsid protein (NC), from an unspecific nucleic acid binding protein (NABP) to an all-in-one viral protein with multiple key functions in the early and late phases of the retrovirus replication cycle, notably reverse transcription of the genomic RNA and viral DNA integration into the host genome, and selection of the genomic RNA together with the initial steps of virus morphogenesis. In this context we will discuss the notion that NC protein has a flexible conformation and is thus a member of the growing family of intrinsically disordered proteins (IDPs) where disorder may account, at least in part, for its function as a nucleic acid (NA) chaperone and possibly as a protein chaperone vis-Ã -vis the viral DNA polymerase during reverse transcription. Lastly, we will briefly review the development of new anti-retroviral/AIDS compounds targeting HIV-1 NC because it represents an ideal target due to its multiple roles in the early and late phases of virus replication and its high degree of conservation.
Keywords
PBSMoMuLVMuLVASLVBLVRetrovirusesLTRnucleocapsidIDPPDBDLSgRNAGenomic RNAIntegraseZinc fingersZinc fingerReverse transcriptaseLong terminal repeatdisPrimer binding sitethree dimensionalMatrixultraviolet lightMurine leukemia virusBovine leukemia virusRetrovirusNucleocapsid proteinProtein Data BankNucleic acid binding proteinIntrinsically disordered proteinCapsid
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Authors
Jean-Luc Darlix, Hugues de Rocquigny, Olivier Mauffret, Yves Mély,