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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.

Author information

1
Tufts Medical Center, Boston, MA, United States.
2
Department of Pathology and Cell Biology, College of Physicians and Surgeons of Columbia University, New York, NY, United States.
3
Tufts University Sackler School of Graduate Medical Sciences, Boston, MA, United States.
4
University of Puerto Rico, Cayey, PR, United States.
#
Contributed equally

Abstract

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.

KEYWORDS:

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

PMID:
23954365
PMCID:
PMC3856541
DOI:
10.1016/j.molbiopara.2013.08.002
[Indexed for MEDLINE]
Free PMC Article

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