Journal article
Plasmodium falciparum subtilisin-like ookinete protein SOPT plays an important and conserved role during ookinete infection of the Anopheles stephensi midgut
JS Armistead, C Jennison, MT O'Neill, S Lopaticki, P Liehl, KK Hanson, T Annoura, P Rajasekaran, SM Erickson, CJ Tonkin, SM Khan, MM Mota, JA Boddey
Molecular Microbiology | WILEY | Published : 2018
DOI: 10.1111/mmi.13993
Abstract
Transmission of the malaria parasite Plasmodium falciparum involves infection of Anopheles mosquitoes. Here we characterize SOPT, a protein expressed in P. falciparum ookinetes that facilitates infection of the mosquito midgut. SOPT was identified on the basis that it contains a signal peptide, a PEXEL-like sequence and is expressed in asexual, ookinete and sporozoite stages, suggesting it is involved in infecting the human or mosquito host. SOPT is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad and is orthologous to P. berghei PIMMS2. Localization studies reveal that SOPT is not exported to the erythrocyte but is expressed in ookinetes at the parasite perip..
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Awarded by National Institutes of Health
Funding Acknowledgements
We thank Ryan Smith (Iowa State University) for helpful discussions regarding SRPN6 expression and the Australian Red Cross Melbourne for human erythrocytes and serum. Monoclonal Antibody 4B7 anti-Plasmodium falciparum 25 kDa Gamete Surface Protein (Pfs25), MRA-28, was obtained through BEI Resources NIAID, NIH, contributed by David C. Kaslow. Anti-aldolase antibodies were a gift from Alan Cowman. This work was supported by the Australian National Health and Medical Research Council (Project Grant 1049811), Human Frontiers Science Program (RGY0073/2012), and a Victorian State Government Operational Infrastructure Support and Australian Government NHMRC IRIISS. JAB was a Queen Elizabeth II Fellow of the Australian Research Council (DP110105395). The funders had no role in study design, data collection, and interpretation, or the decision to submit the work for publication.