biostudies-literaturePaluszynski JNIH trainingNIAID NIH HHSNIH114-21https://www.ebi.ac.uk/biostudies/studies/S-EPMC4073680biostudies-literatureUnknown193(2)Cryptosporidium spp. are intracellular apicomplexan parasites that cause outbreaks of waterborne diarrheal disease worldwide. Previous studies had identified a Cryptosporidium parvum sporozoite antigen, CpMuc4, that appeared to be involved in attachment and invasion of the parasite into intestinal epithelial cells. CpMuc4 is predicted to be O- and N-glycosylated and the antigen exhibits an apparent molecular weight 10kDa larger than the antigen expressed in Escherichia coli, indicative of post-translational modifications. However, lectin blotting and enzymatic and chemical deglycosylation did not identify any glycans on the native antigen. Expression of CpMuc4 in Toxoplasma gondii produced a recombinant protein of a similar molecular weight to the native antigen. Both purified native CpMucMolecular and biochemical parasitologyBiochemical and functional characterization of CpMuc4, a Cryptosporidium surface antigen that binds to host epithelial cells.PMC4073680T32 AI007329R21AI081643 and R21AI081643-02S1R21AI081643-02S1R21 AI081643T32AI007329R21AI081643Williams MMorris CMonahan ZBurns PO'Connor RPaluszynski JLai OfalseBiochemical and functional characterization of CpMuc4, a Cryptosporidium surface antigen that binds to host epithelial cells.Cryptosporidium spp. are intracellular apicomplexan parasites that cause outbreaks of waterborne diarrheal disease worldwide. Previous studies had identified a Cryptosporidium parvum sporozoite antigen, CpMuc4, that appeared to be involved in attachment and invasion of the parasite into intestinal epithelial cells. CpMuc4 is predicted to be O- and N-glycosylated and the antigen exhibits an apparent molecular weight 10kDa larger than the antigen expressed in Escherichia coli, indicative of post-translational modifications. However, lectin blotting and enzymatic and chemical deglycosylation did not identify any glycans on the native antigen. Expression of CpMuc4 in Toxoplasma gondii produced a recombinant protein of a similar molecular weight to the native antigen. Both purified native CpMuc2014-01-01T00:00:00Z2014 Feb2026-05-02T11:10:12.361Z2019-03-27T01:30:59ZS-EPMC40736802469074010.1016/j.molbiopara.2014.03.005