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TitleRepeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenic E. coli adhesin.
Journal, issue, pagesPLoS Pathog, Vol. 20, Issue 9, Page e1012241, Year 2024
Publish dateSep 16, 2024
AuthorsZachary T Berndsen / Marjahan Akhtar / Mahima Thapa / Tim J Vickers / Aaron Schmitz / Jonathan L Torres / Sabyasachi Baboo / Pardeep Kumar / Nazia Khatoon / Alaullah Sheikh / Melissa Hamrick / Jolene K Diedrich / Salvador Martinez-Bartolome / Patrick T Garrett / John R Yates / Jackson S Turner / Renee M Laird / Frédéric Poly / Chad K Porter / Jeffrey Copps / Ali H Ellebedy / Andrew B Ward / James M Fleckenstein /
PubMed AbstractEnterotoxigenic Escherichia coli (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 ...Enterotoxigenic Escherichia coli (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 volunteers challenged with ETEC, diarrheal severity is significantly increased 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 volunteers with ETEC. To understand how EtpA directs ETEC-blood group A interactions and stimulates adaptive immunity, we mutated EtpA, mapped its glycosylation by mass-spectrometry (MS), isolated polyclonal (pAbs) and monoclonal antibodies (mAbs) from vaccinated mice and ETEC-infected volunteers, and determined structures of antibody-EtpA complexes by cryo-electron microscopy. Both bgA and mAbs that inhibited EtpA-bgA interactions and ETEC adhesion, bound to the C-terminal repeat domain highlighting this region as crucial for ETEC pathogen-host interaction. MS analysis uncovered extensive and heterogeneous N-linked glycosylation of EtpA and cryo-EM structures revealed that mAbs directly engage these unique glycan containing epitopes. Finally, electron microscopy-based polyclonal epitope mapping revealed antibodies targeting numerous distinct epitopes on N and C-terminal domains, suggesting that EtpA vaccination generates responses against neutralizing and decoy regions of the molecule. Collectively, we anticipate that these data will inform our general understanding of pathogen-host glycan interactions and adaptive immunity relevant to rational vaccine subunit design.
External linksPLoS Pathog / PubMed:39283948 / PubMed Central
MethodsEM (single particle)
Resolution3.97 Å
Structure data

43119

8vbb

EMDB-43119, PDB-8vbb:
The secreted adhesin EtpA of Enterotoxigenic Escherichia coli in complex with the mouse mAb 1G05
Method: EM (single particle) / Resolution: 3.97 Å

Chemicals

ChemComp-BGC:
beta-D-glucopyranose

Source
  • escherichia coli etec h10407 (bacteria)
  • mus musculus (house mouse)
KeywordsCELL ADHESION / Adhesin / glycoprotein / lectin / antibody-antigen complex

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