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Mol Biochem Parasitol. 2013 Sep;191(1):24-7. doi: 10.1016/j.molbiopara.2013.08.002. Epub 2013 Aug 13.

Identification of a family of four UDP-polypeptide N-acetylgalactosaminyl transferases in Cryptosporidium species.

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Tufts Medical Center, Boston, MA, United States.
Department of Pathology and Cell Biology, College of Physicians and Surgeons of Columbia University, New York, NY, United States.
Tufts University Sackler School of Graduate Medical Sciences, Boston, MA, United States.
University of Puerto Rico, Cayey, PR, United States.
Contributed equally


Although mucin-type O-glycans are critical for Cryptosporidium infection, the enzymes catalyzing their synthesis have not been studied. Here, we report four UDP N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyl transferases (ppGalNAc-Ts) from the genomes of C. parvum, C. hominis and C. muris. All are Type II membrane proteins which include a cytoplasmic tail, a transmembrane domain, a stem region, a glycosyltransferase family 2 domain and a C-terminal ricin B lectin domain. All are expressed during C. parvum infection in vitro, with Cp-ppGalNAc-T1 and -T4 expressed at 24 h and Cp-ppGalNAc-T2 and -T3 at 48 and 72 h post-infection, suggesting that their expression may be developmentally regulated. C. parvum sporozoite lysates display ppGalNAc-T enzymatic activity against non-glycosylated and pre-glycosylated peptides suggesting that they contain enzymes capable of glycosylating both types of substrates. The importance of mucin-type O-glycans in Cryptosporidium-host cell interactions raises the possibility that Cp-ppGalNAc-Ts may serve as targets for intervention in cryptosporidiosis.


Cryptosporidium; Mucin; Mucin-like glycoprotein; O-glycosylation; UDP GalNAc:polypeptide N-acetylgalactosaminyl transferase

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