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Article

Structural rewiring of the mannose-binding pocket reveals adaptive FimH mutations that enhance uroplakin-associated glycan recognition and uropathogenic adhesion.

International journal of biological macromolecules - 1 Jun 2026

Shekhar Shashank, Bhagat Khushboo, Padhi Aditya K

Abstract excerpt

Urinary tract infections are a major global health burden, with uropathogenic Escherichia coli (UPEC) as the leading causative agent. UPEC adhesion is mediated by the fimbrial lectin FimH, which recognizes high-mannose glycans on the urothelial uroplakin (UPK) complex. While FimH interactions with isolated glycans are structurally characterized, its recognition of UPK1A-tethered glycans within the intact human...

Topics

Adhesins, Escherichia coli
Fimbriae Proteins
Mannose
Humans
Polysaccharides
Uropathogenic Escherichia coli
Animals
Mutation
Binding Sites
Bacterial Adhesion
Protein Binding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Swine

Urinary Tract Infections

Source

Identifiers

PMID: 42097418
DOI: 10.1016/j.ijbiomac.2026.152407

Genes

MBP
UPK1A

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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