PrP^C has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1 - 23/03/08

Edmund Derrington ^a, Caroline Gabus ^a, Pascal Leblanc ^a, Jonas Chnaidermann ^a, Linda Grave ^a, Dominique Dormont ^b, Wieslaw Swietnicki ^c, Manuel Morillas ^c, Daniel Marck ^d, Pradip Nandi ^d, Jean-Luc Darlix ^a,⁎
^a Laboretro, unité de virologie humaine, Inserm-ENS U412, ENS de Lyon, 46, allée d'Italie, 69364 Lyon, France
^b Département de Recherche Médicale, CEA, BP 6, 92265 Fontenay-aux-Roses, France
^c Department of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA
^d Inra, centre de recherche de Tours, 37380 Nouzilly, France

^*Correspondence and reprints

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Abstract

The function of the cellular prion protein (PrP^C) remains obscure. Studies suggest that PrP^C functions in several processes including signal transduction and Cu²⁺ metabolism. PrP^C has also been established to bind nucleic acids. Therefore we investigated the properties of PrP^C as a putative nucleic acid chaperone. Surprisingly, PrP^C possesses all the nucleic acid chaperoning properties previously specific to retroviral nucleocapsid proteins. PrP^C appears to be a molecular mimic of NCP7, the nucleocapsid protein of HIV-1. Thus PrP^C, like NCP7, chaperones the annealing of tRNA^Lys to the HIV-1 primer binding site, the initial step of retrovirus replication. PrP^C also chaperones the two DNA strand transfers required for production of a complete proviral DNA with LTRs. Concerning the functions of NCP7 during budding, PrP^C also mimics NCP7 by dimerizing the HIV-1 genomic RNA. These data are unprecedented because, although many cellular proteins have been identified as nucleic acid chaperones, none have the properties of retroviral nucleocapsid proteins. To cite this article: E. Derrington et al., C. R. Biologies 325 (2002) 17-23.

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Keywords : prion, nucleic acid chaperone, nucleocapsid protein, HIV-1

Plan

Introduction

Functions of the cellular prion protein (PrP^C)

Nucleic acid chaperone functions of NCP7

Results

PrP mimics NCP7 chaperone activity in tRNA^Lys annealing and initiation of ss-cDNA synthesis by RT

PrP mimics NCP7 during strand transfers required to generate LTRs of HIV-1 proviral DNA

PrP mimics NCP7 with respect to the inhibition of self-primed reverse transcription

PrP mimics NCP7 with respect to the dimerization of HIV-1 genomic RNA

Discussion

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Vol 325 - N° 1

P. 17-23 - janvier 2002 Retour au numéro

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PrP^C has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1 - 23/03/08

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