Conservation, abundance, glycosylation profile, and localization of the TSP protein family in Cryptosporidium parvum
- Author(s)
- John, A; Bader, SM; Madiedo Soler, N; Wiradiputri, K; Tichkule, S; Smyth, ST; Ralph, SA; Jex, AR; Scott, NE; Tonkin, CJ; Goddard-Borger, ED;
- Details
- Publication Year 2023-02-10,Volume 299,Issue #3,Page 103006
- Journal Title
- Journal of Biological Chemistry
- Abstract
- Cryptosporidium parvum is a zoonotic apicomplexan parasite and a common cause of diarrheal disease worldwide. The development of vaccines to prevent or limit infection remains an important goal for tackling cryptosporidiosis. At present, the only approved vaccine against any apicomplexan parasite targets a conserved adhesin possessing a thrombospondin repeat (TSR) domain. C. parvum possesses 12 orthologous TSR domain-containing proteins known as CpTSP1-12, though little is known about these potentially important antigens. Here, we explore the architecture and conservation of the CpTSP protein family, as well as their abundance at the protein level within the sporozoite stage of the lifecycle. We examine the glycosylation states of these proteins using a combination of antibody-enabled and ZIC-HILIC enrichment techniques, to demonstrate that these proteins are modified with C-, O-, and N-linked glycans. Using expansion microscopy, and an antibody against the C-linked mannose that is unique to the CpTSP protein family within C. parvum, we show that these proteins are found both on the cell surface and in structures that resemble the secretory pathway of C. parvum sporozoites. Finally, we generated a polyclonal antibody against CpTSP1 (TRAP-C1) to show that it is found at the cell surface and within micronemes, in a pattern reminiscent of other apicomplexan motility-associated adhesins, and is present both in sporozoites and meronts. This work sheds new light on an under-studied family of C. parvum proteins that are likely to be important to both parasite biology and the development of vaccines against cryptosporidiosis.
- Publisher
- Elsevier
- Research Division(s)
- Chemical Biology; Structural Biology; Infectious Diseases And Immune Defence; Population Health And Immunity
- PubMed ID
- 36775128
- Publisher's Version
- https://doi.org/10.1016/j.jbc.2023.103006
- Open Access at Publisher's Site
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Creation Date: 2023-03-17 11:09:09
Last Modified: 2023-03-27 05:04:09