A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions]
Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q.
The American Society for Microbiology (ASM)
Published 2018
The American Society for Microbiology (ASM)
Published 2018
| Publication Date: |
2018-07-24
|
|---|---|
| Publisher: |
The American Society for Microbiology (ASM)
|
| Print ISSN: |
0019-9567
|
| Electronic ISSN: |
1098-5522
|
| Topics: |
Medicine
|
| Published by: |
| _version_ | 1836399011796353024 |
|---|---|
| autor | Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. |
| beschreibung | Invasion of erythrocytes by merozoites is required in the life cycle of malarial parasites. Proteins derived from the invasive merozoites are essential ligands for erythrocyte recognition and penetration. In this study, we report a novel protein that possesses a Trx domain-like structure of the thioredoxin family and is expressed on the surface of merozoites of the malaria parasite Plasmodium falciparum . This protein, namely, PfTrx-mero protein, displayed a mutated sequence character at the Trx domain, but with a specific binding activity to human erythrocytes. Specific antibodies to the protein inhibited merozoite invasion into human erythrocytes. Immunization with a homologous protein of Plasmodium berghei strain ANKA also showed significant protection against lethal infection in mice. These results suggested that the novel PfTrx-like-mero protein expressed on the surface of merozoites is an important ligand participating in erythrocyte invasion and a potential vaccine candidate. |
| citation_standardnr | 6308026 |
| datenlieferant | ipn_articles |
| feed_id | 519 |
| feed_publisher | The American Society for Microbiology (ASM) |
| feed_publisher_url | http://www.asm.org/ |
| insertion_date | 2018-07-24 |
| journaleissn | 1098-5522 |
| journalissn | 0019-9567 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | The American Society for Microbiology (ASM) |
| quelle | Infection and Immunity |
| relation | http://iai.asm.org/cgi/content/short/86/8/e00289-18?rss=1 |
| search_space | articles |
| shingle_author_1 | Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. |
| shingle_author_2 | Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. |
| shingle_author_3 | Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. |
| shingle_author_4 | Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. |
| shingle_catch_all_1 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] Invasion of erythrocytes by merozoites is required in the life cycle of malarial parasites. Proteins derived from the invasive merozoites are essential ligands for erythrocyte recognition and penetration. In this study, we report a novel protein that possesses a Trx domain-like structure of the thioredoxin family and is expressed on the surface of merozoites of the malaria parasite Plasmodium falciparum . This protein, namely, PfTrx-mero protein, displayed a mutated sequence character at the Trx domain, but with a specific binding activity to human erythrocytes. Specific antibodies to the protein inhibited merozoite invasion into human erythrocytes. Immunization with a homologous protein of Plasmodium berghei strain ANKA also showed significant protection against lethal infection in mice. These results suggested that the novel PfTrx-like-mero protein expressed on the surface of merozoites is an important ligand participating in erythrocyte invasion and a potential vaccine candidate. Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. The American Society for Microbiology (ASM) 0019-9567 00199567 1098-5522 10985522 |
| shingle_catch_all_2 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] Invasion of erythrocytes by merozoites is required in the life cycle of malarial parasites. Proteins derived from the invasive merozoites are essential ligands for erythrocyte recognition and penetration. In this study, we report a novel protein that possesses a Trx domain-like structure of the thioredoxin family and is expressed on the surface of merozoites of the malaria parasite Plasmodium falciparum . This protein, namely, PfTrx-mero protein, displayed a mutated sequence character at the Trx domain, but with a specific binding activity to human erythrocytes. Specific antibodies to the protein inhibited merozoite invasion into human erythrocytes. Immunization with a homologous protein of Plasmodium berghei strain ANKA also showed significant protection against lethal infection in mice. These results suggested that the novel PfTrx-like-mero protein expressed on the surface of merozoites is an important ligand participating in erythrocyte invasion and a potential vaccine candidate. Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. The American Society for Microbiology (ASM) 0019-9567 00199567 1098-5522 10985522 |
| shingle_catch_all_3 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] Invasion of erythrocytes by merozoites is required in the life cycle of malarial parasites. Proteins derived from the invasive merozoites are essential ligands for erythrocyte recognition and penetration. In this study, we report a novel protein that possesses a Trx domain-like structure of the thioredoxin family and is expressed on the surface of merozoites of the malaria parasite Plasmodium falciparum . This protein, namely, PfTrx-mero protein, displayed a mutated sequence character at the Trx domain, but with a specific binding activity to human erythrocytes. Specific antibodies to the protein inhibited merozoite invasion into human erythrocytes. Immunization with a homologous protein of Plasmodium berghei strain ANKA also showed significant protection against lethal infection in mice. These results suggested that the novel PfTrx-like-mero protein expressed on the surface of merozoites is an important ligand participating in erythrocyte invasion and a potential vaccine candidate. Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. The American Society for Microbiology (ASM) 0019-9567 00199567 1098-5522 10985522 |
| shingle_catch_all_4 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] Invasion of erythrocytes by merozoites is required in the life cycle of malarial parasites. Proteins derived from the invasive merozoites are essential ligands for erythrocyte recognition and penetration. In this study, we report a novel protein that possesses a Trx domain-like structure of the thioredoxin family and is expressed on the surface of merozoites of the malaria parasite Plasmodium falciparum . This protein, namely, PfTrx-mero protein, displayed a mutated sequence character at the Trx domain, but with a specific binding activity to human erythrocytes. Specific antibodies to the protein inhibited merozoite invasion into human erythrocytes. Immunization with a homologous protein of Plasmodium berghei strain ANKA also showed significant protection against lethal infection in mice. These results suggested that the novel PfTrx-like-mero protein expressed on the surface of merozoites is an important ligand participating in erythrocyte invasion and a potential vaccine candidate. Wang, W., Huang, P., Jiang, N., Lu, H., Zhang, D., Wang, D., Zhang, K., Wahlgren, M., Chen, Q. The American Society for Microbiology (ASM) 0019-9567 00199567 1098-5522 10985522 |
| shingle_title_1 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] |
| shingle_title_2 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] |
| shingle_title_3 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] |
| shingle_title_4 | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] |
| timestamp | 2025-06-30T23:36:11.937Z |
| titel | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] |
| titel_suche | A Thioredoxin Homologous Protein of Plasmodium falciparum Participates in Erythrocyte Invasion [Cellular Microbiology: Pathogen-Host Cell Molecular Interactions] |
| topic | WW-YZ |
| uid | ipn_articles_6308026 |