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Author Wang, Ying ♦ Dang, Xiaoqun ♦ Luo, Bo ♦ Li, Chunfeng ♦ Long, Mengxian ♦ Li, Tian ♦ Li, Zhi ♦ Pan, Guoqing ♦ Zhou, Zeyang
Source SpringerLink
Content type Text
Publisher Springer Berlin Heidelberg
File Format PDF
Copyright Year ©2015
Language English
Subject Domain (in DDC) Technology ♦ Medicine & health
Subject Keyword Microsporidia ♦ Deubiquitinating enzymes ♦ Otubain-like protease ♦ Nosema bombycis ♦ Medical Microbiology ♦ Microbiology ♦ Immunology
Abstract Otubains are a recently identified family of deubiquitinating enzymes (DUBs). They are involved in diverse biological processes including protein degradation, signal transduction, and cell immune response. Several microsporidian genomes have been published in the last decade; however, little is known about the otubain-like protease in these widely-spread obligate intracellular parasites. Here, we characterized a 25 kDa otubain-like protease (NbOTU1) from the microsporidian Nosema bombycis, the pathogen causing pebrine disease in the economically important insect Bombyx mori. Sequence analysis showed that this protein contained a conserved catalytic triad of otubains composed of aspartate, cysteine, and histidine residues. The expression of Nbotu1 began on day 3 postinfection as determined by the RT-PCR method. Immunofluorescence analysis indicated that NbOTU1 is localized on the spore wall of N. bombycis. The subcellular localization of the NbOTU1 was further detected with immunoelectron microscopy, which showed that NbOTU1 is localized at the regions around endospore wall and plasma membrane. Deubiquitination analysis confirmed that the recombinant NbOTU1 possessed deubiquitination activity in vitro. Taken together, a novel microsporidian otubain-like protease NbOTU1 was partially characterized in N. bombycis, demonstrating its subcellular location and deubiquitination activity. This study provided a basic reference for further dissecting the function of otubains in microsporidia.
ISSN 09320113
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2015-07-17
Publisher Place Berlin/Heidelberg
e-ISSN 14321955
Journal Parasitology Research
Volume Number 114
Issue Number 10
Page Count 8
Starting Page 3759
Ending Page 3766

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Source: SpringerLink