<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Berndsen ZT</submitter><funding>BLRD VA</funding><funding>NIAID NIH HHS</funding><pubmed_abstract>Enterotoxigenic &lt;i>Escherichia coli&lt;/i> (ETEC) cause hundreds of millions of cases of infectious diarrhea annually, predominantly in children from low-middle income regions. Notably, in children, as well as human volunteers challenged with ETEC, diarrheal severity is significantly increased severity in blood group A (bgA) individuals. EtpA, is a secreted glycoprotein adhesin that functions as a blood group A lectin to promote critical interactions between ETEC and blood group A glycans on intestinal epithelia for effective bacterial adhesion and toxin delivery. EtpA is highly immunogenic resulting in robust antibody responses following natural infection and experimental challenge of human volunteers with ETEC. To understand how EtpA directs ETEC-blood group A interactions and stimulates ad</pubmed_abstract><journal>bioRxiv : the preprint server for biology</journal><pagination>2024.05.08.593125</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11100705</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenic &lt;i>E. coli adhesin&lt;/i>.</pubmed_title><pmcid>PMC11100705</pmcid><funding_grant_id>T32 AI007172</funding_grant_id><funding_grant_id>R01 AI089894</funding_grant_id><funding_grant_id>R01 AI126887</funding_grant_id><funding_grant_id>I01 BX001469</funding_grant_id><pubmed_authors>Poly F</pubmed_authors><pubmed_authors>Laird RM</pubmed_authors><pubmed_authors>Vickers T</pubmed_authors><pubmed_authors>Turner JS</pubmed_authors><pubmed_authors>Thapa M</pubmed_authors><pubmed_authors>Ellebedy AH</pubmed_authors><pubmed_authors>Sheikh A</pubmed_authors><pubmed_authors>Diedrich JK</pubmed_authors><pubmed_authors>Baboo S</pubmed_authors><pubmed_authors>Kumar P</pubmed_authors><pubmed_authors>Khatoom N</pubmed_authors><pubmed_authors>Torres JL</pubmed_authors><pubmed_authors>Fleckenstein JM</pubmed_authors><pubmed_authors>Schmitz A</pubmed_authors><pubmed_authors>Martinez-Bartolome S</pubmed_authors><pubmed_authors>Garrett PT</pubmed_authors><pubmed_authors>Yates JR</pubmed_authors><pubmed_authors>Hamrick M</pubmed_authors><pubmed_authors>Berndsen ZT</pubmed_authors><pubmed_authors>Akhtar M</pubmed_authors><pubmed_authors>Porter CK</pubmed_authors><pubmed_authors>Copps J</pubmed_authors><pubmed_authors>Ward AB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenic &lt;i>E. coli adhesin&lt;/i>.</name><description>Enterotoxigenic &lt;i>Escherichia coli&lt;/i> (ETEC) cause hundreds of millions of cases of infectious diarrhea annually, predominantly in children from low-middle income regions. Notably, in children, as well as human volunteers challenged with ETEC, diarrheal severity is significantly increased severity in blood group A (bgA) individuals. EtpA, is a secreted glycoprotein adhesin that functions as a blood group A lectin to promote critical interactions between ETEC and blood group A glycans on intestinal epithelia for effective bacterial adhesion and toxin delivery. EtpA is highly immunogenic resulting in robust antibody responses following natural infection and experimental challenge of human volunteers with ETEC. To understand how EtpA directs ETEC-blood group A interactions and stimulates ad</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 May</publication><modification>2026-07-03T03:23:50.152Z</modification><creation>2026-07-03T03:14:50.158Z</creation></dates><accession>S-EPMC11100705</accession><cross_references><pubmed>38766097</pubmed><doi>10.1101/2024.05.08.593125</doi></cross_references></HashMap>