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Int J Parasitol. 2017 Jun;47(7):409-423. doi: 10.1016/j.ijpara.2016.10.002. Epub 2016 Nov 27.

The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle.

Author information

1
Center for Infectious Disease Research, formerly Seattle Biomedical Research Institute, Seattle, WA, USA.
2
Center for Infectious Disease Research, formerly Seattle Biomedical Research Institute, Seattle, WA, USA; Department of Global Health, University of Washington, Seattle, WA, USA. Electronic address: stefan.kappe@cidresearch.org.

Abstract

During their life cycle Plasmodium parasites rely upon an arsenal of proteins that establish key interactions with the host and 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 localise at the parasite surface or interface with the host and vector, 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.

KEYWORDS:

6-cys proteins; Adhesion proteins; Host-pathogen interactions; Malaria; Malaria vaccine; Plasmodium; s48/45

PMID:
27899328
PMCID:
PMC5446806
DOI:
10.1016/j.ijpara.2016.10.002
[Indexed for MEDLINE]
Free PMC Article

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