Clone, expression and plasminogen binding property of three fructose-1,6-bisphosphate aldolases from Clonorchis sinensis
https://doi.org/10.47665/tb.37.4.852
- Author:
Li, S.
1
,
2
,
3
;
Lu, B.P.
1
;
Feng, J.
4
;
Zhou, J.J.
5
;
Xie, Z.Z.
6
;
Liang, C.
2
,
3
;
Li, X.R.
2
,
3
;
Huang, Y.
2
,
3
;
Yu, X.B.
2
,
3
Author Information
1. School of Basic Medicine, Henan University of Chinese Medicine, Zhengzhou 450046, China&
2. Department of Parasitology, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou 510080, China&
3. Key Laboratory for Tropical Diseases Control of Ministry of Education, Sun Yat-sen University, Guangzhou 510080, China
4. Zhengzhou YIHE Hospital Affiliated to Henan University, Zhengzhou 450047, China
5. Zhengzhou Key Laboratory for Childrens Infection and Immunity, Childrens Hospital Affiliated to Zhengzhou University, Zhengzhou 450047, China
6. Department of Clinical Laboratory, Third Affiliated Hospital of Sun Yat sen University, Guangzhou 510630, China
- Publication Type:Journal Article
- From:Tropical Biomedicine
2020;37(No.4):852-863
- CountryMalaysia
- Language:English
-
Abstract:
Fructose-1,6-bisphosphate aldolase (FbA), a well characterized glycometabolism
enzyme, has been found to participate in other important processes besides the classic
catalysis. To understand the important functions of three fructose-1,6-bisphosphate aldolases
from Clonorchis sinensis (CsFbAs, CsFbA-1/2/3) in host-parasite interplay, the open reading
frames of CsFbAs were cloned into pET30a (+) vector and the resulting recombinant plasmids
were transformed into Escherichia coli BL21 (DE3) for expression of the proteins. Purified
recombinant CsFbAs proteins (rCsFbAs) were approximately 45.0 kDa on 12% SDS-PAGE and
could be probed with each rat anti-rCsFbAs sera by western blotting analysis. ELISA and
ligand blot overlay indicated that rCsFbAs of 45.0 kDa as well as native CsFbAs of 39.5 kDa
from total worm extracts and excretory-secretory products of Clonorchis sinensis (CsESPs)
could bind to human plasminogen, and the binding could be efficiently inhibited by lysine
analog ε-aminocaproic acid. Our results suggested that as both the components of CsESPs
and the plasminogen binding proteins, three CsFbAs might be involved in preventing the
formation of the blood clot so that Clonorchis sinensis could acquire enough nutrients from
host tissue for their successful survival and colonization in the host. Our work will provide us
with new information about the biological function of three CsFbAs and their roles in hostparasite interplay
- Full text:8.2020my1170.pdf
