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Structural, biochemical, and in vivo characterization of the first virally encoded cyclophilin from the Mimivirus.

Abstract：

:Although multiple viruses utilize host cell cyclophilins, including severe acute respiratory syndrome (SARS) and human immunodeficiency virus type-1(HIV-1), their role in infection is poorly understood. To help elucidate these roles, we have characterized the first virally encoded cyclophilin (mimicyp) derived from the largest virus discovered to date (the Mimivirus) that is also a causative agent of pneumonia in humans. Mimicyp adopts a typical cyclophilin-fold, yet it also forms trimers unlike any previously characterized homologue. Strikingly, immunofluorescence assays reveal that mimicyp localizes to the surface of the mature virion, as recently proposed for several viruses that recruit host cell cyclophilins such as SARS and HIV-1. Additionally mimicyp lacks peptidyl-prolyl isomerase activity in contrast to human cyclophilins. Thus, this study suggests that cyclophilins, whether recruited from host cells (i.e. HIV-1 and SARS) or virally encoded (i.e. Mimivirus), are localized on viral surfaces for at least a subset of viruses.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Thai V,Renesto P,Fowler CA,Brown DJ,Davis T,Gu W,Pollock DD,Kern D,Raoult D,Eisenmesser EZ

doi

10.1016/j.jmb.2007.08.051

subject

Has Abstract

pub_date

2008-04-18 00:00:00

pages

71-86

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(07)01132-1

journal_volume

378

pub_type

杂志文章

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