TY - JOUR
T1 - The biochemical and functional characterization of M28 aminopeptidase protein secreted by Acanthamoeba spp. On host cell interaction
AU - Huang, Jian Ming
AU - Chang, Yao Tsung
AU - Lin, Wei Chen
N1 - Funding Information:
Funding: This research was supported by the Ministry of Science and Technology (MOST) to WCL (grant MOST 106-2320-B-006-070-MY3).
Funding Information:
This research was supported by the Ministry of Science and Technology (MOST) to WCL (grant MOST 106-2320-B-006-070-MY3). We acknowledge Professor Woei-Jer Chuang and Jyh-Wei Shin for providing reagents/materials/analysis tools.
Publisher Copyright:
© 2019 by the authors.
PY - 2019/12/13
Y1 - 2019/12/13
N2 - Acanthamoeba are a free-living protozoan whose pathogenic strain can cause severe human diseases, such as granulomatous encephalitis and keratitis. As such, the pathogenic mechanism between humans and Acanthamoeba is still unknown. In our previous study, we identified the secreted Acanthamoeba M28 aminopeptidase (M28AP) and then suggested that M28AP can degrade human C3b and iC3b for inhibiting the destruction of Acanthamoeba spp. with the human immune response. We constructed the produced the recombinant M28AP from a CHO cell, which is a mammalian expression system, to characterize the biochemical properties of Acanthamoeba M28AP. The recombinant M28AP more rapidly hydrolyzed Leu-AMC than Arg-AMC and could be inhibited by EDTA treatment. We show that recombinant M28AP can be delivered into the individual cell line and cause cell line apoptosis in a co-culture model. In conclusion, we successfully investigated the potential molecular characteristics of M28AP.
AB - Acanthamoeba are a free-living protozoan whose pathogenic strain can cause severe human diseases, such as granulomatous encephalitis and keratitis. As such, the pathogenic mechanism between humans and Acanthamoeba is still unknown. In our previous study, we identified the secreted Acanthamoeba M28 aminopeptidase (M28AP) and then suggested that M28AP can degrade human C3b and iC3b for inhibiting the destruction of Acanthamoeba spp. with the human immune response. We constructed the produced the recombinant M28AP from a CHO cell, which is a mammalian expression system, to characterize the biochemical properties of Acanthamoeba M28AP. The recombinant M28AP more rapidly hydrolyzed Leu-AMC than Arg-AMC and could be inhibited by EDTA treatment. We show that recombinant M28AP can be delivered into the individual cell line and cause cell line apoptosis in a co-culture model. In conclusion, we successfully investigated the potential molecular characteristics of M28AP.
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U2 - 10.3390/molecules24244573
DO - 10.3390/molecules24244573
M3 - Article
C2 - 31847255
AN - SCOPUS:85076631623
VL - 24
JO - Molecules
JF - Molecules
SN - 1420-3049
IS - 24
M1 - 4573
ER -