scholarly journals Biochemical analysis of a sugar 4,6‐dehydratase from Acanthamoeba polyphaga Mimivirus

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

Characterization of an aminotransferase from Acanthamoeba polyphaga Mimivirus

2021 ◽  
Author(s):  
Chase A. Seltzner ◽  
Justin D. Ferek ◽  
James B. Thoden ◽  
Hazel M. Holden
Keyword(s):  
Acanthamoeba Polyphaga ◽  
Acanthamoeba Polyphaga Mimivirus

scholarly journals Ultrastructural Characterization of the Giant Volcano-like Virus Factory of Acanthamoeba polyphaga Mimivirus

PLoS ONE ◽  
2007 ◽  
Vol 2 (3) ◽  
pp. e328 ◽  
Author(s):  
Marie Suzan-Monti ◽  
Bernard La Scola ◽  
Lina Barrassi ◽  
Leon Espinosa ◽  
Didier Raoult
Keyword(s):  
Acanthamoeba Polyphaga ◽  
Ultrastructural Characterization ◽  
Acanthamoeba Polyphaga Mimivirus ◽  
Virus Factory

scholarly journals Acanthamoeba polyphaga Mimivirus Prevents Amoebal Encystment-Mediating Serine Proteinase Expression and Circumvents Cell Encystment

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 ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Giant Virus ◽  
Acanthamoeba Polyphaga ◽  
Free Living ◽  
Content Type ◽  
Acanthamoeba Polyphaga Mimivirus

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.

scholarly journals Giant mimivirus R707 encodes a glycogenin paralogue polymerizing glucose through α- and β-glycosidic linkages

2016 ◽  
Vol 473 (20) ◽  
pp. 3451-3462 ◽  
Author(s):  
Anna J. Rommel ◽  
Andreas J. Hülsmeier ◽  
Simon Jurt ◽  
Thierry Hennet
Keyword(s):  
Metal Ion ◽  
Divalent Metal ◽  
Open Reading Frame ◽  
Homologous Gene ◽  
Acanthamoeba Polyphaga ◽  
Reading Frame ◽  
Cellular Life ◽  
Divalent Metal Ion ◽  
Nucleotide Sugars ◽  
Acanthamoeba Polyphaga Mimivirus

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.

scholarly journals Distinct DNA Exit and Packaging Portals in the Virus Acanthamoeba polyphaga mimivirus

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

scholarly journals The high‐resolution structure of a UDP‐L‐rhamnose synthase from Acanthamoeba polyphaga Mimivirus

2020 ◽  
Vol 29 (11) ◽  
pp. 2164-2174
Author(s):  
Nicholas J. Bockhaus ◽  
Justin D. Ferek ◽  
James B. Thoden ◽  
Hazel M. Holden
Keyword(s):  
High Resolution ◽  
Acanthamoeba Polyphaga ◽  
High Resolution Structure ◽  
Acanthamoeba Polyphaga Mimivirus ◽  
Resolution Structure

scholarly journals The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRSapm ) is a monomer in solution

FEBS Letters ◽  
2013 ◽  
Vol 587 (6) ◽  
pp. 590-599 ◽  
Author(s):  
Aparajita Choudhury ◽  
Rajat Banerjee
Keyword(s):  
Trna Synthetase ◽  
Acanthamoeba Polyphaga ◽  
Terminal Fragment ◽  
Acanthamoeba Polyphaga Mimivirus

Pneumonia in mice inoculated experimentally with Acanthamoeba polyphaga mimivirus

2007 ◽  
Vol 42 (2-3) ◽  
pp. 56-61 ◽  
Author(s):  
Mohammad Khan ◽  
Bernard La Scola ◽  
Hubert Lepidi ◽  
Didier Raoult
Keyword(s):  
Acanthamoeba Polyphaga ◽  
Acanthamoeba Polyphaga Mimivirus
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