PMID- 33622724
OWN - NLM
STAT- MEDLINE
DCOM- 20210909
LR  - 20211028
IS  - 2150-7511 (Electronic)
VI  - 12
IP  - 1
DP  - 2021 Feb 23
TI  - Discovery of Bacterial Fimbria-Glycan Interactions Using Whole-Cell Recombinant 
      Escherichia coli Expression.
LID - 10.1128/mBio.03664-20 [doi]
LID - e03664-20
AB  - Chaperone-usher (CU) fimbriae are the most abundant Gram-negative bacterial 
      fimbriae, with 38 distinct CU fimbria types described in Escherichia coli alone. 
      Some E. coli CU fimbriae have been well characterized and bind to specific glycan 
      targets to confer tissue tropism. For example, type 1 fimbriae bind to 
      alpha-d-mannosylated glycoproteins such as uroplakins in the bladder via their 
      tip-located FimH adhesin, leading to colonization and invasion of the bladder 
      epithelium. Despite this, the receptor-binding affinity of many other E. coli CU 
      fimbria types remains poorly characterized. Here, we used a recombinant E. coli 
      strain expressing different CU fimbriae, in conjunction with glycan array 
      analysis comprising >300 glycans, to dissect CU fimbria receptor specificity. We 
      initially validated the approach by demonstrating the purified FimH 
      lectin-binding domain and recombinant E. coli expressing type 1 fimbriae bound to 
      a similar set of glycans. This technique was then used to map the glycan binding 
      affinity of six additional CU fimbriae, namely, P, F1C, Yqi, Mat/Ecp, K88, and 
      K99 fimbriae. The binding affinity was determined using whole-bacterial-cell 
      surface plasmon resonance. This work describes new information in fimbrial 
      specificity and a rapid and scalable system to define novel adhesin-glycan 
      interactions that underpin bacterial colonization and disease.IMPORTANCE 
      Understanding the tropism of pathogens for host and tissue requires a complete 
      understanding of the host receptors targeted by fimbrial adhesins. Furthermore, 
      blocking adhesion is a promising strategy to counter increasing antibiotic 
      resistance and is enabled by the identification of host receptors. Here, we use a 
      defined E. coli heterologous expression system to identify glycan receptors for 
      six chaperone-usher fimbriae and identify novel receptors that are consistent 
      with their known function. The same system was used to measure the kinetics of 
      binding to the identified glycan, wherein bacterial cells were immobilized onto a 
      biosensor chip and the interactions with glycans were quantified by surface 
      plasmon resonance. This novel, dual-level analysis, where screening for the 
      repertoire of glycan binding and the hierarchy of affinity of the identified 
      ligands is determined directly from a natively expressed fimbrial structure on 
      the bacterial cell surface, is superior in both throughput and biological 
      relevance.
CI  - Copyright (c) 2021 Day et al.
FAU - Day, Christopher J
AU  - Day CJ
AD  - Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
FAU - Lo, Alvin W
AU  - Lo AW
AD  - School of Chemistry and Molecular Biosciences, The University of Queensland, 
      Brisbane, Australia.
AD  - Australian Infectious Diseases Research Centre, The University of Queensland, 
      Brisbane, Australia.
FAU - Hartley-Tassell, Lauren E
AU  - Hartley-Tassell LE
AD  - Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
FAU - Argente, M Pilar
AU  - Argente MP
AD  - Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
FAU - Poole, Jessica
AU  - Poole J
AD  - Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
FAU - King, Nathan P
AU  - King NP
AD  - School of Chemistry and Molecular Biosciences, The University of Queensland, 
      Brisbane, Australia.
AD  - Australian Infectious Diseases Research Centre, The University of Queensland, 
      Brisbane, Australia.
FAU - Tiralongo, Joe
AU  - Tiralongo J
AD  - Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
FAU - Jennings, Michael P
AU  - Jennings MP
AUID- ORCID: 0000-0002-1027-4684
AD  - Institute for Glycomics, Griffith University, Gold Coast, Queensland, Australia 
      m.jennings@griffith.edu.au m.schembri@uq.edu.au.
FAU - Schembri, Mark A
AU  - Schembri MA
AUID- ORCID: 0000-0003-4863-9260
AD  - School of Chemistry and Molecular Biosciences, The University of Queensland, 
      Brisbane, Australia m.jennings@griffith.edu.au m.schembri@uq.edu.au.
AD  - Australian Infectious Diseases Research Centre, The University of Queensland, 
      Brisbane, Australia.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20210223
PL  - United States
TA  - mBio
JT  - mBio
JID - 101519231
RN  - 0 (Adhesins, Escherichia coli)
RN  - 0 (Polysaccharides)
RN  - 147680-16-8 (Fimbriae Proteins)
SB  - IM
MH  - Adhesins, Escherichia coli/metabolism
MH  - *Bacterial Adhesion
MH  - Escherichia coli/*genetics/metabolism
MH  - Fimbriae Proteins/*genetics/metabolism
MH  - Fimbriae, Bacterial/genetics/*metabolism
MH  - Kinetics
MH  - Polysaccharides/*metabolism
MH  - Protein Binding
PMC - PMC8545135
OTO - NOTNLM
OT  - Escherichia coli
OT  - FimH
OT  - fimbriae
OT  - glycomics
OT  - glycoproteins
EDAT- 2021/02/25 06:00
MHDA- 2021/09/10 06:00
PMCR- 2021/02/23
CRDT- 2021/02/24 05:36
PHST- 2021/02/24 05:36 [entrez]
PHST- 2021/02/25 06:00 [pubmed]
PHST- 2021/09/10 06:00 [medline]
PHST- 2021/02/23 00:00 [pmc-release]
AID - mBio.03664-20 [pii]
AID - mBio03664-20 [pii]
AID - 10.1128/mBio.03664-20 [doi]
PST - epublish
SO  - mBio. 2021 Feb 23;12(1):e03664-20. doi: 10.1128/mBio.03664-20.