Target antigens of malaria transmission blocking immunity exist as a stable membrane bound complex

By Nirbhay Kumar. 1987

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1. Silvia A. Arredondo
2. Frankie M. T. Lyons
3. Mikha Gabriela
4. Stefan H. I. Kappe
5. M. V. van Dijk
6. Ben C. L. van Schaijk
7. K. Miura
8. M. Tonkin

Citations in the corpus

• The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle (2016, background): “Pfs230 and Pfs48/45 were initially co-eluted with these transmission-blocking mAbs, and thus the two proteins were characterized in parallel in the early experiments and were soon found to interact with each other (Kumar, 1987; Kumar and Wizel, 1992).”
• Three Members of the 6-cys Protein Family of Plasmodium Play a Role in Gamete Fertility (2010, background): “falciparum evidence has been found that P230 forms a complex with P48/45 at the surface of gametocytes and gametes [18,27,59,60].”
• Malaria transmission‐blocking antigen, Pfs230, mediates human red blood cell binding to exflagellating male parasites and oocyst production (2006, result): “…for Pfs48/45 to retain Pfs230 on the gamete surface is consistent with previous Pfs230/Pfs48/45 co-immunoprecipitation data and the presence of a glycosylphosphatidylinositol anchor addition signal at the C-terminus of Pfs48/45, not Pfs230 (Kumar, 1987; Kumar and Wizel, 1992; Kocken et al., 1993).”
• Structure of the Pf12 and Pf41 heterodimeric complex of Plasmodium falciparum 6-cysteine proteins (2022, background): “Pfs48/45 is GPI-anchored and forms a stable complex with secreted Pfs230 (Kumar 1987, Kumar and Wizel 1992).”
• Structure of the Plasmodium 6-cysteine s48/45 domain (2012, background): “Pfs230 is a soluble protein that associates with the gamete membrane by binding to Pfs48/45 (15).”
• Plasmodium 6-Cysteine Proteins: Functional Diversity, Transmission-Blocking Antibodies and Structural Scaffolds (2022, background): “A genetically attenuated parasite (GAP) vaccine with deletions of Pf36, Pf52 and another liver stage antigen SAP1 has undergone a Phase I clinical trial (NCT03168854), and was able to elicit antibodies that inhibited sporozoite invasion and traversal (Kublin et al., 2017).”
• Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies (2022, background): “This flexibility may allow Pfs48/45 to adopt different conformations on binding to partners, such as Pfs230 and will also leave all three domains exposed to antibody recognition.”
• Structural and Immunological Characterization of Recombinant 6-Cysteine Domains of the Plasmodium falciparum Sexual Stage Protein Pfs230* (2016, background): “Pfs230 forms a complex with Pfs48/45, a glycosylphosphatidylinositol anchored protein (15) on the surface of sexual stage parasites (16, 17).”
• Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41* (2013, background): “Although Pf12, Pf38, and Pf92 are associated with the membrane through a GPI4 anchor (20), it was recently established that soluble Pf41 (17) heterodimerizes with Pf12 to maintain membrane association (21), similar to the association of soluble Pfs230withGPIanchored Pfs48/45 (7, 22).”