The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle
By Silvia A. Arredondo, Stefan H. I. Kappe. 2016
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During their life cycle Plasmodium parasites rely upon an arsenal of proteins that establish key interactions with the host or vector, and between the parasite sexual stages, with the purpose of ensuring infection, reproduction and proliferation. Among these is a group of secreted or membrane-anchored proteins known as the six-cysteine (6-cys) family. This is a small but important family with only 14 members thus far identified, each stage-specifically expressed during the parasite life cycle. 6-cys proteins often localize at the parasite surface or interface with the host and are conserved in different Plasmodium species. The unifying feature of the family is the s48/45 domain, presumably involved in adhesion and structurally related to Ephrins, the ligands of Eph receptors. The most prominent s48/45 members are currently under functional investigation and are being pursued as vaccine candidates. In this review, we examine what is known about the 6-cys family, their structure and function, and discuss future research directions.
Subfields: Immunology, Oncology, Public Health, Environmental and Occupational Health
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Citations in the corpus
- Plasmodium 6-Cysteine Proteins: Functional Diversity, Transmission-Blocking Antibodies and Structural Scaffolds (2022, background): “, 2005) of the asexual blood stages, as well as on gametocytes, gametes and zygotes (Feller et al., 2013; Arredondo and Kappe, 2017).”
- Identification of domains within Pfs230 that elicit transmission blocking antibody responses (2019, unknown): “Analysis of Pfs230 sequences suggests that it is comprised of repeated domains characteristic of 6-cys family proteins [18].”