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Lookup NU author(s): Dr David Bolam, Professor Frank SargentORCiD, Professor Tracy Palmer FRS FRSE FMedSciORCiD, Dr Emmanuele SeveriORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Sialic acid (Sia) transporters are critical to the capacity of host-associated bacteria to utilise Sia for growth and/or cell surface modification. While N-acetyl-neuraminic acid (Neu5Ac)-specific transporters have been studied extensively, little is known on transporters dedicated to anhydro-Sia forms such as 2,7-anhydro-Neu5Ac (2,7-AN) or 2,3-dehydro-2-deoxy-Neu5Ac (Neu5Ac2en). Here, we used a Sia-transport-null strain of Escherichia coli to investigate the function of members of anhydro-Sia transporter families previously identified by computational studies. First, we showed that the transporter NanG, from the Glycoside-Pentoside-Hexuronide:cation symporter family, is a specific 2,7-AN transporter, and identified by mutagenesis a crucial functional residue within the putative substrate-binding site. We then demonstrated that NanX transporters, of the Major Facilitator Superfamily, also only transport 2,7-AN and not Neu5Ac2en nor Neu5Ac. Finally, we provided evidence that SiaX transporters, of the Sodium-Solute Symporter superfamily, are promiscuous Neu5Ac/Neu5Ac2en transporters able to acquire either substrate equally well. The characterisation of anhydro-Sia transporters expands our current understanding of prokaryotic Sia metabolism within host-associated microbial communities.
Author(s): Wu Y, Bell A, Thomas GH, Bolam DN, Sargent F, Juge N, Palmer T, Severi E
Publication type: Article
Publication status: Published
Journal: Microbiology
Year: 2024
Volume: 170
Issue: 3
Online publication date: 15/03/2024
Acceptance date: 29/02/2024
Date deposited: 02/04/2024
ISSN (print): 1350-0872
ISSN (electronic): 1465-2080
Publisher: The Microbiology Society
URL: https://doi.org/10.1099/mic.0.001448
DOI: 10.1099/mic.0.001448
PubMed id: 38488830
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