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The Structure and Dynamics of BmR1 Protein from Brugia malayi: In Silico Approaches
Brugia malayi is a filarial nematode, which causes lymphatic filariasis in humans. In 1995, the disease has been identified by the World Health Organization (WHO) as one of the second leading causes of permanent and long-term disability and thus it is targeted for elimination by year 2020. Therefore...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4100200/ https://www.ncbi.nlm.nih.gov/pubmed/24950179 http://dx.doi.org/10.3390/ijms150611082 |
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author | Khor, Bee Yin Tye, Gee Jun Lim, Theam Soon Noordin, Rahmah Choong, Yee Siew |
author_facet | Khor, Bee Yin Tye, Gee Jun Lim, Theam Soon Noordin, Rahmah Choong, Yee Siew |
author_sort | Khor, Bee Yin |
collection | PubMed |
description | Brugia malayi is a filarial nematode, which causes lymphatic filariasis in humans. In 1995, the disease has been identified by the World Health Organization (WHO) as one of the second leading causes of permanent and long-term disability and thus it is targeted for elimination by year 2020. Therefore, accurate filariasis diagnosis is important for management and elimination programs. A recombinant antigen (BmR1) from the Bm17DIII gene product was used for antibody-based filariasis diagnosis in “Brugia Rapid”. However, the structure and dynamics of BmR1 protein is yet to be elucidated. Here we study the three dimensional structure and dynamics of BmR1 protein using comparative modeling, threading and ab initio protein structure prediction. The best predicted structure obtained via an ab initio method (Rosetta) was further refined and minimized. A total of 5 ns molecular dynamics simulation were performed to investigate the packing of the protein. Here we also identified three epitopes as potential antibody binding sites from the molecular dynamics average structure. The structure and epitopes obtained from this study can be used to design a binder specific against BmR1, thus aiding future development of antigen-based filariasis diagnostics to complement the current diagnostics. |
format | Online Article Text |
id | pubmed-4100200 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-41002002014-07-16 The Structure and Dynamics of BmR1 Protein from Brugia malayi: In Silico Approaches Khor, Bee Yin Tye, Gee Jun Lim, Theam Soon Noordin, Rahmah Choong, Yee Siew Int J Mol Sci Article Brugia malayi is a filarial nematode, which causes lymphatic filariasis in humans. In 1995, the disease has been identified by the World Health Organization (WHO) as one of the second leading causes of permanent and long-term disability and thus it is targeted for elimination by year 2020. Therefore, accurate filariasis diagnosis is important for management and elimination programs. A recombinant antigen (BmR1) from the Bm17DIII gene product was used for antibody-based filariasis diagnosis in “Brugia Rapid”. However, the structure and dynamics of BmR1 protein is yet to be elucidated. Here we study the three dimensional structure and dynamics of BmR1 protein using comparative modeling, threading and ab initio protein structure prediction. The best predicted structure obtained via an ab initio method (Rosetta) was further refined and minimized. A total of 5 ns molecular dynamics simulation were performed to investigate the packing of the protein. Here we also identified three epitopes as potential antibody binding sites from the molecular dynamics average structure. The structure and epitopes obtained from this study can be used to design a binder specific against BmR1, thus aiding future development of antigen-based filariasis diagnostics to complement the current diagnostics. MDPI 2014-06-19 /pmc/articles/PMC4100200/ /pubmed/24950179 http://dx.doi.org/10.3390/ijms150611082 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Khor, Bee Yin Tye, Gee Jun Lim, Theam Soon Noordin, Rahmah Choong, Yee Siew The Structure and Dynamics of BmR1 Protein from Brugia malayi: In Silico Approaches |
title | The Structure and Dynamics of BmR1 Protein from Brugia malayi: In
Silico Approaches |
title_full | The Structure and Dynamics of BmR1 Protein from Brugia malayi: In
Silico Approaches |
title_fullStr | The Structure and Dynamics of BmR1 Protein from Brugia malayi: In
Silico Approaches |
title_full_unstemmed | The Structure and Dynamics of BmR1 Protein from Brugia malayi: In
Silico Approaches |
title_short | The Structure and Dynamics of BmR1 Protein from Brugia malayi: In
Silico Approaches |
title_sort | structure and dynamics of bmr1 protein from brugia malayi: in
silico approaches |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4100200/ https://www.ncbi.nlm.nih.gov/pubmed/24950179 http://dx.doi.org/10.3390/ijms150611082 |
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