NDLI: Cloning, expression, and partial characterization of FBPA from Schistosoma japonicum, a molecule on that the fluke may develop nutrition competition and immune evasion from human

Content Provider	Springer Nature Link
Author	Hu, Qiping Xie, Huiqiong Zhu, Shuyu Liao, Dejun Zhan, Tingzheng Liu, Dengyu
Copyright Year	2015
Abstract	Carbohydrate metabolism is the most important physiological process for Schistosoma japonicum which resides in host. However, as a key glycolytic enzyme in carbohydrate metabolism, fructose-1,6-bisphosphate aldolase (FBPA), there is no study on its enzymatic kinetics and antigenic peptides. Here, we report the gene cloning, expression, purification, and kinetics of the FBPA from S. japonicum (sjFBPA). After cloning, sjFBPA gene was introduced into pET-28a and transformed BL21, and a soluble His6-sjFBPA was expressed and purified successfully at the expected molecular mass of ~45 kDa. We first reported that the diversities in IGS regions and the features of residues position 346 and 357–362 of sjFBPA may be conferred either through conformational changes influencing easily the active site from a distance and/or causing the C-terminal region to interact directly with the active site, which lead His6-sjFBPA to exhibit a higher specific activity of 197.43 units/mg and degrades FBP with a typical substrate inhibition model and a higher efficiency of k cat = 6261.3/s and K m = 0.061 μM than human aldolases, which might be the strategy that S. japonicum gaining energy and surviving in its environment with low concentration of carbohydrate, and benefitting to get more metabolic substances for parasites in nutrition competition with their host. sjFBPA exhibits a high similarity of 81.46 % with that of hosts, especially in antigenic peptide regions, and 14 of 15 antigenic peptides of sjFBPA were conserved to those of human aldolase A, B, and/or C with high identity (17, 16, or 16 antigenic peptides, respectively), which may result in a molecular mimicry of FBPA with that of host, and an immune evasion from their hosts. This work would supply an experimental base for using FBPA to prevent the schistosomiasis in the future.
Starting Page	3459
Ending Page	3468
Page Count	10
File Format	PDF
ISSN	09320113
Journal	Parasitology Research
Volume Number	114
Issue Number	9
e-ISSN	14321955
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2015-06-24
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Schistosoma japonicum Fructose-1,6-bisphosphate aldolase Cloning Expression Enzymatic kinetics Antigenic peptide Substrate inhibition Medical Microbiology Microbiology Immunology
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Veterinary Parasitology Insect Science

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Pcal_0111, a highly thermostable bifunctional fructose-1,6-bisphosphate aldolase/phosphatase from Pyrobaculum calidifontis

MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity

Structure of Tagatose-1,6-bisphosphate Aldolase INSIGHT INTO CHIRAL DISCRIMINATION, MECHANISM, AND SPECIFICITY OF CLASS II ALDOLASES

Evaluation of recombinant fructose-1,6-bisphosphate aldolase ELISA test for the diagnosis of Schistosoma japonicum in water buffaloes.

Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis

Diagnosis of schistosomiasis using recombinant fructose-1,6-bisphosphate aldolase from a Formosan strain of Schistosoma japonicum.

Structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi.

Characterization of recombinant fructose-1,6-bisphosphate aldolase from Methylococcus capsulatus Bath

Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate

Cloning, expression, and partial characterization of FBPA from Schistosoma japonicum, a molecule on that the fluke may develop nutrition competition and immune evasion from human

Similar Documents

Pcal_0111, a highly thermostable bifunctional fructose-1,6-bisphosphate aldolase/phosphatase from Pyrobaculum calidifontis

MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity

Structure of Tagatose-1,6-bisphosphate Aldolase INSIGHT INTO CHIRAL DISCRIMINATION, MECHANISM, AND SPECIFICITY OF CLASS II ALDOLASES

Evaluation of recombinant fructose-1,6-bisphosphate aldolase ELISA test for the diagnosis of Schistosoma japonicum in water buffaloes.

Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis

Diagnosis of schistosomiasis using recombinant fructose-1,6-bisphosphate aldolase from a Formosan strain of Schistosoma japonicum.

Structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi.

Characterization of recombinant fructose-1,6-bisphosphate aldolase from Methylococcus capsulatus Bath

Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate

Cloning, expression, and partial characterization of FBPA from Schistosoma japonicum, a molecule on that the fluke may develop nutrition competition and immune evasion from human