{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nesta B"],"funding":["NIAID NIH HHS"],"pagination":["e1004124"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4014459"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(5)"],"pubmed_abstract":["SslE, the Secreted and surface-associated lipoprotein from Escherichia coli, has recently been associated to the M60-like extracellular zinc-metalloprotease sub-family which is implicated in glycan recognition and processing. SslE can be divided into two main variants and we recently proposed it as a potential vaccine candidate. By applying a number of in vitro bioassays and comparing wild type, knockout mutant and complemented strains, we have now demonstrated that SslE specifically contributes to degradation of mucin substrates, typically present in the intestine and bladder. Mutation of the zinc metallopeptidase motif of SslE dramatically impaired E. coli mucinase activity, confirming the specificity of the phenotype observed. Moreover, antibodies raised against variant I SslE, cloned f"],"journal":["PLoS pathogens"],"pubmed_title":["SslE elicits functional antibodies that impair in vitro mucinase activity and in vivo colonization by both intestinal and extraintestinal Escherichia coli strains."],"pmcid":["PMC4014459"],"funding_grant_id":["R01 AI043363","R01 AI43363"],"pubmed_authors":["Nesta B","Bertoldi I","Seib KL","Soriani M","Mora M","Buccato S","Mobley HL","Rippa V","Rosini R","Donato P","Serino L","Bensi G","Del Vecchio M","Pezzicoli A","Buzzigoli L","Ashhab Y","Fontana MR","Alteri CJ","Spagnuolo A","Valeri M","Pizza M","Tuscano G","Falduto M"],"additional_accession":[]},"is_claimable":false,"name":"SslE elicits functional antibodies that impair in vitro mucinase activity and in vivo colonization by both intestinal and extraintestinal Escherichia coli strains.","description":"SslE, the Secreted and surface-associated lipoprotein from Escherichia coli, has recently been associated to the M60-like extracellular zinc-metalloprotease sub-family which is implicated in glycan recognition and processing. SslE can be divided into two main variants and we recently proposed it as a potential vaccine candidate. By applying a number of in vitro bioassays and comparing wild type, knockout mutant and complemented strains, we have now demonstrated that SslE specifically contributes to degradation of mucin substrates, typically present in the intestine and bladder. Mutation of the zinc metallopeptidase motif of SslE dramatically impaired E. coli mucinase activity, confirming the specificity of the phenotype observed. Moreover, antibodies raised against variant I SslE, cloned f","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 May","modification":"2026-05-04T23:27:40.718Z","creation":"2019-03-26T22:43:03Z"},"accession":"S-EPMC4014459","cross_references":{"pubmed":["24809621"],"doi":["10.1371/journal.ppat.1004124"]}}