{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Paluszynski J"],"funding":["NIH training","NIAID NIH HHS","NIH"],"pagination":["114-21"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4073680"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["193(2)"],"pubmed_abstract":["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 CpMuc"],"journal":["Molecular and biochemical parasitology"],"pubmed_title":["Biochemical and functional characterization of CpMuc4, a Cryptosporidium surface antigen that binds to host epithelial cells."],"pmcid":["PMC4073680"],"funding_grant_id":["T32 AI007329","R21AI081643 and R21AI081643-02S1","R21AI081643-02S1","R21 AI081643","T32AI007329","R21AI081643"],"pubmed_authors":["Williams M","Morris C","Monahan Z","Burns P","O'Connor R","Paluszynski J","Lai O"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical and functional characterization of CpMuc4, a Cryptosporidium surface antigen that binds to host epithelial cells.","description":"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 CpMuc","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Feb","modification":"2026-05-02T11:10:12.361Z","creation":"2019-03-27T01:30:59Z"},"accession":"S-EPMC4073680","cross_references":{"pubmed":["24690740"],"doi":["10.1016/j.molbiopara.2014.03.005"]}}