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Titolo:
Antibody inhibition of the transcriptase activity of the rotavirus DLP: A structural view
Autore:
Thouvenin, E; Schoehn, G; Rey, F; Petitpas, I; Mathieu, M; Vaney, MC; Cohen, J; Kohli, E; Pothier, P; Hewat, E;
Indirizzi:
Inst Biol Struct, F-38027 Grenoble, France Inst Biol Struct Grenoble France F-38027 truct, F-38027 Grenoble, France CNRS, UPR 9053, Lab Genet Virus, F-91198 Gif Sur Yvette, France CNRS Gif Sur Yvette France F-91198 Virus, F-91198 Gif Sur Yvette, France INRA, CRJ, Lab Virol & Immunol Mol, F-78350 Jouy En Josas, France INRA Jouy En Josas France F-78350 nol Mol, F-78350 Jouy En Josas, France Univ Bourgogne, UFR Med & Pharm, Lab Microbiol Med & Mol, F-21000 Dijon, France Univ Bourgogne Dijon France F-21000 iol Med & Mol, F-21000 Dijon, France
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 307, anno: 2001,
pagine: 161 - 172
SICI:
0022-2836(20010316)307:1<161:AIOTTA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYOELECTRON MICROSCOPY; NEUTRALIZING ANTIBODY; 3-DIMENSIONAL STRUCTURE; MONOCLONAL-ANTIBODIES; IMAGE-RECONSTRUCTION; CRYSTAL-STRUCTURE; IN-VITRO; VIRUS; PROTEIN; PARTICLES;
Keywords:
cryo-electron microscopy; monoclonal antibodies; rotavirus; transcription; X-ray crystallography;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Hewat, E Inst Biol Struct, 41 Rue Jules Horowitz, F-38027 Grenoble, FranceInst Biol Struct 41 Rue Jules Horowitz Grenoble France F-38027 e
Citazione:
E. Thouvenin et al., "Antibody inhibition of the transcriptase activity of the rotavirus DLP: A structural view", J MOL BIOL, 307(1), 2001, pp. 161-172

Abstract

On entering the host cell the rotavirus virion loses its outer shell to become a double-layered particle (DLP). The DLP then transcribes the 11 segments of its dsRNA genome using its own transcriptase complex, and the maturemRNA emerges along the 5-fold axis. Ln order to better understand the transcription mechanism and the role of VP6 in transcription we have studied three monoclonal antibodies against VP6: RV-238 which inhibits the transcriptase activity of the DLP; and RV-133 and RV138 which have no effect on transcription. The structures obtained by cryo-electron microscopy of the DLP/Fab complexes and by X-ray crystallography of the VP6 trimer and the VP6/Fab-238 complex have been combined to give pseudo-atomic structures. Steric hindrance between the Fabs results in limited Fab occupancy. In particular, there are on average only three of a possible five Fabs-238 which point towards the 5-fold axis. Thus, Fabs-238 are not in a position to block the exiting mRNA, nor is there any visible conformational change in VP6 on antibody binding at a resolution of 23 Angstrom. However, the epitope of the inhibiting antibody involves two VP6 monomers, whereas, those of the non-inhibiting antibodies have an epitope on only one VP6. Thus, the inhibition of transcription may be a result of inhibition of a possible change in the VP6 conformation associated with the transcription of mRNA. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 01:26:32