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Fig. 1 | Parasites & Vectors

Fig. 1

From: The mucin-like, secretory type-I transmembrane glycoprotein GP900 in the apicomplexan Cryptosporidium parvum is cleaved in the secretory pathway and likely plays a lubrication role

Fig. 1

Architecture of the mucin-like Cryptosporidium parvum GP900 protein. The protein contains an N-terminal SP for targeting the protein to the endoplasmic reticulum and a TMD near the C-terminus to separate the long non-cytoplasmic domain and the short cytoplasmic domain. There are 10 intrinsic disorder regions with various lengths across the protein (brown), numerous sites for O-glycosylation, including two long threonine (Thr)-rich regions (green), a number of sites for N-glycosylation (blue), and 15 cysteine (Cys) residues (red). Sites recognized by the mouse anti-GP900-N monoclonal antibody (mAb) and the rabbit anti-GP900-polyclonal antibody (pAb) are also marked (purple). Abbreviations: SP, signal peptide; TMD, transmembrane domain

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