Home | My Profile | Contact Us
Research Trends Products  |   order gateway  |   author gateway  |   editor gateway  
Register | Forgot Password

Author Resources
 Author Gateway
 Article submission guidelines

Editor Resources
 Editor/Referee Gateway

 Regional Subscription Agents/Distributors
Current Topics in Peptide & Protein Research   Volumes    Volume 19 
Cloning and protein structure prediction of DBL2β-PfEMP1 recombinant protein from Indonesian Plasmodium falciparum isolate
Erma Sulistyaningsih, Fathul Hidayah, Aris Prasetyo
Pages: 75 - 79
Number of pages: 5
Current Topics in Peptide & Protein Research
Volume 19 

Copyright © 2018 Research Trends. All rights reserved

The DBL2β-PfEMP1 is an adhesive domain of Plasmodium falciparum, which is important for malaria pathogenesis. In this study, the DBL2β-PfEMP1 from the Indonesian isolate of Plasmodium falciparum was cloned and the protein structure prediction of the DBL2β recombinant protein as well as its ligand binding sites was carried out. The DBL2β recombinant protein consists of 1674 nucleotides which are translated into 558 amino acids. Analysis using Expasy ProtParam tool showed that the protein had a MW of 64.69 kDa with an isoelectric point of 8.82. It had 83 negatively charged residues (Asp + Glu) and 98 positively charged residues (Arg + Lys). It was classified as an unstable protein because it had an instability index of 40.01. Protein structure prediction of the DBL2β recombinant protein and its binding sites was carried out using the I-TASSER program. It showed that the DBL2β recombinant protein had the highest significant alignment with the DBLβ domain of PF11_0521 PfEMP1, which is bound to the human ICAM-1, but the protein had the closest structural similarity with the of EBA-175 Region II (RII) of P.  falciparum, where the protein functions as the cell invasion molecule. The highest C-score of ligand-binding site was 0.10 for the PEPTIDE ligand (GLN, LEU, ASP, PHE, GLU, ASP, VAL, TRP, ASN, SER, SER, TYR), and the ligand-binding site residues were at 84, 87, 88, 91, 92, 95, 99, 196, 199, 200, 203, 206. It is likely that the DBL2β recombinant protein has the major function as an adhesion molecule for invasion to the host. Further studies on its role in in vivo models are needed to develop a definite conclusion.
View Full Article  


Buy this article
Buy this volume
Subscribe to this title
Shopping Cart

Quick Links
Search Products
Browse in Alphabetical Order : Journals
Browse by Subject Classification : Journals

Ordering Information Ordering Information
Downloadable forms Downloadable Forms