ArticleInternational journal of molecular sciences2014
The structure and dynamics of BmR1 protein from Brugia malayi: in silico approaches.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
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- Is the Glycoprotein Responsible for the Differences in Dispersal Rates between Lettuce Necrotic Yellows Virus Subgroups?Viruses · 2022Article
- Characterization of a novel microfilarial antigen for diagnosis of Wuchereria bancrofti infections.PLoS neglected tropical diseases · 2022Article
- Recombinant antigens used as diagnostic tools for lymphatic filariasis.Parasites & vectors · 2021Review
- Review
- Structure of cytotoxic associated antigen A protein ofVeterinary world · 2020Article
- Designing a less immunogenic nattokinase from Bacillus subtilis subsp. natto: a computational mutagenesis.Journal of molecular modeling · 2019Article
- Metazoan Parasite Vaccines: Present Status and Future Prospects.Frontiers in cellular and infection microbiology · 2018Review
- General overview on structure prediction of twilight-zone proteins.Theoretical biology & medical modelling · 2015Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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