SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector
The SAS6-like (SAS6L) protein, a truncated paralogue of the ubiquitous basal body/centriole protein SAS6, has been characterised recently as a flagellum protein in trypanosomatids, but associated with the conoid in apicomplexan Toxoplasma. The conoid has been suggested to derive from flagella parts,...
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| Format: | Article |
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Nature Publishing Group
2016
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| Online Access: | https://eprints.nottingham.ac.uk/34207/ |
| _version_ | 1848794798520008704 |
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| author | Wall, Richard J. Roques, Magali Katris, Nicholas J. Koreny, Ludek Stanway, Rebecca R. Brady, Declan Waller, Ross F. Tewari, Rita |
| author_facet | Wall, Richard J. Roques, Magali Katris, Nicholas J. Koreny, Ludek Stanway, Rebecca R. Brady, Declan Waller, Ross F. Tewari, Rita |
| author_sort | Wall, Richard J. |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | The SAS6-like (SAS6L) protein, a truncated paralogue of the ubiquitous basal body/centriole protein SAS6, has been characterised recently as a flagellum protein in trypanosomatids, but associated with the conoid in apicomplexan Toxoplasma. The conoid has been suggested to derive from flagella parts, but is thought to have been lost from some apicomplexans including the malaria-causing genus Plasmodium. Presence of SAS6L in Plasmodium, therefore, suggested a possible role in flagella assembly in male gametes, the only flagellated stage. Here, we have studied the expression and role of SAS6L throughout the Plasmodium life cycle using the rodent malaria model P. berghei. Contrary to a hypothesised role in flagella, SAS6L was absent during gamete flagellum formation. Instead, SAS6L was restricted to the apical complex in ookinetes and sporozoites, the extracellular invasive stages that develop within the mosquito vector. In these stages SAS6L forms an apical ring, as we show is also the case in Toxoplasma tachyzoites. The SAS6L ring was not apparent in blood-stage invasive merozoites, indicating that the apical complex is differentiated between the different invasive forms. Overall this study indicates that a conoid-associated apical complex protein and ring structure is persistent in Plasmodium in a stage-specific manner. |
| first_indexed | 2025-11-14T19:21:55Z |
| format | Article |
| id | nottingham-34207 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:21:55Z |
| publishDate | 2016 |
| publisher | Nature Publishing Group |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-342072020-05-04T17:57:54Z https://eprints.nottingham.ac.uk/34207/ SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector Wall, Richard J. Roques, Magali Katris, Nicholas J. Koreny, Ludek Stanway, Rebecca R. Brady, Declan Waller, Ross F. Tewari, Rita The SAS6-like (SAS6L) protein, a truncated paralogue of the ubiquitous basal body/centriole protein SAS6, has been characterised recently as a flagellum protein in trypanosomatids, but associated with the conoid in apicomplexan Toxoplasma. The conoid has been suggested to derive from flagella parts, but is thought to have been lost from some apicomplexans including the malaria-causing genus Plasmodium. Presence of SAS6L in Plasmodium, therefore, suggested a possible role in flagella assembly in male gametes, the only flagellated stage. Here, we have studied the expression and role of SAS6L throughout the Plasmodium life cycle using the rodent malaria model P. berghei. Contrary to a hypothesised role in flagella, SAS6L was absent during gamete flagellum formation. Instead, SAS6L was restricted to the apical complex in ookinetes and sporozoites, the extracellular invasive stages that develop within the mosquito vector. In these stages SAS6L forms an apical ring, as we show is also the case in Toxoplasma tachyzoites. The SAS6L ring was not apparent in blood-stage invasive merozoites, indicating that the apical complex is differentiated between the different invasive forms. Overall this study indicates that a conoid-associated apical complex protein and ring structure is persistent in Plasmodium in a stage-specific manner. Nature Publishing Group 2016-06-03 Article PeerReviewed Wall, Richard J., Roques, Magali, Katris, Nicholas J., Koreny, Ludek, Stanway, Rebecca R., Brady, Declan, Waller, Ross F. and Tewari, Rita (2016) SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector. Scientific Reports . ISSN 2045-2322 http://www.nature.com/articles/srep28604 doi:10.1038/srep28604 doi:10.1038/srep28604 |
| spellingShingle | Wall, Richard J. Roques, Magali Katris, Nicholas J. Koreny, Ludek Stanway, Rebecca R. Brady, Declan Waller, Ross F. Tewari, Rita SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| title | SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| title_full | SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| title_fullStr | SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| title_full_unstemmed | SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| title_short | SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| title_sort | sas6-like protein in plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector |
| url | https://eprints.nottingham.ac.uk/34207/ https://eprints.nottingham.ac.uk/34207/ https://eprints.nottingham.ac.uk/34207/ |