The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein
Abstract Background Erythrocyte invasion by Plasmodium falciparum parasites represents a key mechanism during malaria pathogenesis. Erythrocyte binding antigen-181 (EBA-181) is an important invasion protein, which mediates a unique host cell entry pathway. A novel interaction between EBA-181 and hum...
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ftdoajarticles:oai:doaj.org/article:414fab2469554636a718c1986a9d29e3 2023-05-15T15:09:33+02:00 The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein Coetzer Theresa L Lanzillotti Roberto 2006-11-01T00:00:00Z https://doi.org/10.1186/1475-2875-5-100 https://doaj.org/article/414fab2469554636a718c1986a9d29e3 EN eng BMC http://www.malariajournal.com/content/5/1/100 https://doaj.org/toc/1475-2875 doi:10.1186/1475-2875-5-100 1475-2875 https://doaj.org/article/414fab2469554636a718c1986a9d29e3 Malaria Journal, Vol 5, Iss 1, p 100 (2006) Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 article 2006 ftdoajarticles https://doi.org/10.1186/1475-2875-5-100 2022-12-31T04:25:15Z Abstract Background Erythrocyte invasion by Plasmodium falciparum parasites represents a key mechanism during malaria pathogenesis. Erythrocyte binding antigen-181 (EBA-181) is an important invasion protein, which mediates a unique host cell entry pathway. A novel interaction between EBA-181 and human erythrocyte membrane protein 4.1 (4.1R) was recently demonstrated using phage display technology. In the current study, recombinant proteins were utilized to define and characterize the precise molecular interaction between the two proteins. Methods 4.1R structural domains (30, 16, 10 and 22 kDa domain) and the 4.1R binding region in EBA-181 were synthesized in specific Escherichia coli strains as recombinant proteins and purified using magnetic bead technology. Recombinant proteins were subsequently used in blot-overlay and histidine pull-down assays to determine the binding domain in 4.1R. Results Blot overlay and histidine pull-down experiments revealed specific interaction between the 10 kDa domain of 4.1R and EBA-181. Binding was concentration dependent as well as saturable and was abolished by heat denaturation of 4.1R. Conclusion The interaction of EBA-181 with the highly conserved 10 kDa domain of 4.1R provides new insight into the molecular mechanisms utilized by P. falciparum during erythrocyte entry. The results highlight the potential multifunctional role of malaria invasion proteins, which may contribute to the success of the pathogenic stage of the parasite's life cycle. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Malaria Journal 5 1 |
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Directory of Open Access Journals: DOAJ Articles |
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ftdoajarticles |
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English |
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Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 |
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Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 Coetzer Theresa L Lanzillotti Roberto The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 |
description |
Abstract Background Erythrocyte invasion by Plasmodium falciparum parasites represents a key mechanism during malaria pathogenesis. Erythrocyte binding antigen-181 (EBA-181) is an important invasion protein, which mediates a unique host cell entry pathway. A novel interaction between EBA-181 and human erythrocyte membrane protein 4.1 (4.1R) was recently demonstrated using phage display technology. In the current study, recombinant proteins were utilized to define and characterize the precise molecular interaction between the two proteins. Methods 4.1R structural domains (30, 16, 10 and 22 kDa domain) and the 4.1R binding region in EBA-181 were synthesized in specific Escherichia coli strains as recombinant proteins and purified using magnetic bead technology. Recombinant proteins were subsequently used in blot-overlay and histidine pull-down assays to determine the binding domain in 4.1R. Results Blot overlay and histidine pull-down experiments revealed specific interaction between the 10 kDa domain of 4.1R and EBA-181. Binding was concentration dependent as well as saturable and was abolished by heat denaturation of 4.1R. Conclusion The interaction of EBA-181 with the highly conserved 10 kDa domain of 4.1R provides new insight into the molecular mechanisms utilized by P. falciparum during erythrocyte entry. The results highlight the potential multifunctional role of malaria invasion proteins, which may contribute to the success of the pathogenic stage of the parasite's life cycle. |
format |
Article in Journal/Newspaper |
author |
Coetzer Theresa L Lanzillotti Roberto |
author_facet |
Coetzer Theresa L Lanzillotti Roberto |
author_sort |
Coetzer Theresa L |
title |
The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein |
title_short |
The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein |
title_full |
The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein |
title_fullStr |
The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein |
title_full_unstemmed |
The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein |
title_sort |
10 kda domain of human erythrocyte protein 4.1 binds the plasmodium falciparum eba-181 protein |
publisher |
BMC |
publishDate |
2006 |
url |
https://doi.org/10.1186/1475-2875-5-100 https://doaj.org/article/414fab2469554636a718c1986a9d29e3 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Malaria Journal, Vol 5, Iss 1, p 100 (2006) |
op_relation |
http://www.malariajournal.com/content/5/1/100 https://doaj.org/toc/1475-2875 doi:10.1186/1475-2875-5-100 1475-2875 https://doaj.org/article/414fab2469554636a718c1986a9d29e3 |
op_doi |
https://doi.org/10.1186/1475-2875-5-100 |
container_title |
Malaria Journal |
container_volume |
5 |
container_issue |
1 |
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1766340725786542080 |