Characterization of an aminotransferase from Acanthamoeba polyphaga Mimivirus

2021 ◽  
Author(s):  
Chase A. Seltzner ◽  
Justin D. Ferek ◽  
James B. Thoden ◽  
Hazel M. Holden
PLoS ONE ◽  
2007 ◽  
Vol 2 (3) ◽  
pp. e328 ◽  
Author(s):  
Marie Suzan-Monti ◽  
Bernard La Scola ◽  
Lina Barrassi ◽  
Leon Espinosa ◽  
Didier Raoult

Viruses ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 312 ◽  
Author(s):  
Clara Rolland ◽  
Julien Andreani ◽  
Amina Louazani ◽  
Sarah Aherfi ◽  
Rania Francis ◽  
...  

The history of giant viruses began in 2003 with the identification of Acanthamoeba polyphaga mimivirus. Since then, giant viruses of amoeba enlightened an unknown part of the viral world, and every discovery and characterization of a new giant virus modifies our perception of the virosphere. This notably includes their exceptional virion sizes from 200 nm to 2 µm and their genomic complexity with length, number of genes, and functions such as translational components never seen before. Even more surprising, Mimivirus possesses a unique mobilome composed of virophages, transpovirons, and a defense system against virophages named Mimivirus virophage resistance element (MIMIVIRE). From the discovery and isolation of new giant viruses to their possible roles in humans, this review shows the active contribution of the University Hospital Institute (IHU) Mediterranee Infection to the growing knowledge of the giant viruses’ field.


2014 ◽  
Vol 89 (5) ◽  
pp. 2962-2965 ◽  
Author(s):  
Paulo Boratto ◽  
Jonas Dutra Albarnaz ◽  
Gabriel Magno de Freitas Almeida ◽  
Lucas Botelho ◽  
Alide Caroline Lima Fontes ◽  
...  

Acanthamoebais a genus of free-living amoebas distributed worldwide. Few studies have explored the interactions between these protozoa and their infecting giant virus,Acanthamoeba polyphagamimivirus (APMV). Here we show that, once the amoebal encystment is triggered, trophozoites become significantly resistant to APMV. Otherwise, upon infection, APMV is able to interfere with the expression of a serine proteinase related to amoebal encystment and the encystment can no longer be triggered.


2016 ◽  
Vol 473 (20) ◽  
pp. 3451-3462 ◽  
Author(s):  
Anna J. Rommel ◽  
Andreas J. Hülsmeier ◽  
Simon Jurt ◽  
Thierry Hennet

Acanthamoeba polyphaga mimivirus is a giant virus encoding 1262 genes among which many were previously thought to be exclusive to cellular life. For example, mimivirus genes encode enzymes involved in the biosynthesis of nucleotide sugars and putative glycosyltransferases. We identified in mimivirus a glycogenin-1 homologous gene encoded by the open reading frame R707. The R707 protein was found to be active as a polymerizing glucosyltransferase enzyme. Like glycogenin-1, R707 activity was divalent-metal-ion-dependent and relied on an intact DXD motif. In contrast with glycogenin-1, R707 was, however, not self-glucosylating. Interestingly, the product of R707 catalysis featured α1-6, β1-6 and α1-4 glycosidic linkages. Mimivirus R707 is the first reported glycosyltransferase able to catalyse the formation of both α and β linkages. Mimivirus-encoded glycans play a role in the infection of host amoebae. Co-infection of Acanthamoeba with mimivirus and amylose and chitin hydrolysate reduced the number of infected amoebae, thus supporting the importance of polysaccharide chains in the uptake of mimivirus by amoebae. The identification of a glycosyltransferase capable of forming α and β linkages underlines the peculiarity of mimivirus and enforces the concept of a host-independent glycosylation machinery in mimivirus.


PLoS Biology ◽  
2008 ◽  
Vol 6 (5) ◽  
pp. e114 ◽  
Author(s):  
Nathan Zauberman ◽  
Yael Mutsafi ◽  
Daniel Ben Halevy ◽  
Eyal Shimoni ◽  
Eugenia Klein ◽  
...  

2020 ◽  
Vol 29 (5) ◽  
pp. 1148-1159 ◽  
Author(s):  
Justin D. Ferek ◽  
James B. Thoden ◽  
Hazel M. Holden

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