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. 2024 Apr 10;14:1367359. doi: 10.3389/fcimb.2024.1367359

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Copyright © 2024 Bertuccini, Boussadia, Salzano, Vanni, Passerò, Nocita, Scaloni, Sanchez, Sargiacomo, Fiani and Tosini

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Cartoon showing some structural features of the Cryptosporidium-characteristic proteins (see text). UniProtKB accessions are reported in brackets. Proteins were divided into three categories according to the presence of hydrophobic motifs (i. e. presence/absence of a signal peptide and/or a transmembrane domain) and their presumptive localization respect to the cell membrane. Prediction of signal peptides and transmembrane domains was performed at Phobius (https://phobius.sbc.su.se/index.html). Prediction of other structural and functional domains was performed at Pfam (http://pfam.xfam.org) and Prosite (https://prosite.expasy.org). List of domains in the figure: Peptidase 1, PEPTIDASE_A1, PS51767; PLP, PROKAR_LIPOPROTEIN, PS51257; CAP, Cysteine-rich secretory protein family, CL0659; GP60, Glycoprotein GP60 of Cryptosporidium, PF11025; PPASE Tensin, PPASE_TENSIN, PS51181; Chase, CHASE, PS50839; DegV, DEGV, PS51482; MyB-L, MYB_LIKE, PS50090; LRR, Leucin Rich Repeat, LRR, PS51450; Thr, Threonin Rich Region, THR_RICH, PS50325; ARM, Armadillo/plakoglobin ARM repeat, ARM_REPEAT, PS50176; CS, CS, PS51203.