Identification of a family of four UDP-polypeptide N-acetylgalactosaminyl transferases in Cryptosporidium species.
Mol Biochem Parasitol
; 191(1): 24-7, 2013 Sep.
Article
en En
| MEDLINE
| ID: mdl-23954365
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-galactosaminepolypeptide 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.
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Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
N-Acetilgalactosaminiltransferasas
/
Cryptosporidium
Tipo de estudio:
Diagnostic_studies
Idioma:
En
Revista:
Mol Biochem Parasitol
Año:
2013
Tipo del documento:
Article