Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/134851
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: Bacteriophage Sf6 host range mutant that infects Shigella flexneri serotype 2a₂ strains
Other Titles: Bacteriophage Sf6 host range mutant that infects Shigella flexneri serotype 2a(2) strains
Author: Teh, M.Y.
Tran, E.N.H.
Morona, R.
Citation: FEMS Microbiology Letters, 2022; 369(1):1-5
Publisher: Oxford University Press (OUP)
Issue Date: 2022
ISSN: 0378-1097
1574-6968
Statement of
Responsibility: 
Min Yan Teh, Elizabeth Ngoc Hoa Tran and Renato Morona
Abstract: Shigella flexneri serotype 2a2 (II:9;10) is the most prevalent strain in causing bacillary dysentery in developing countries. Chemical modifications such as glucosylation, O-acetylation, and phosphoethanolamine modifications of lipopolysaccharide (LPS) O antigen (Oag) contribute to the emergence of various serotypes. Sf6 is a Shigella-specific bacteriophage that infects only a limited range of S. flexneri serotypes [X, Y]. LPS Oag is the primary receptor for bacteriophage Sf6 where it uses its tailspike protein (TSP) in binding and hydrolysing LPS Oags. Sf6TSP has recently been shown to be capable of hydrolysing the LPS Oag of Type II strains, albeit modestly. Phage therapy has regained attention in recent years as an alternative therapeutic approach. Therefore, this study aimed to expand the host range of Sf6 to the prevalent S. flexneri serotype 2a2 strain. We discovered a new lytic Sf6 host range mutant that is capable of infecting S. flexneri serotype 2a2 and identified residues in Sf6TSP that may potentially be involved in binding and hydrolysing serotype 2a2 LPS Oag. This work increased the limited Shigella-specific bacteriophage collection and may be useful in the future for phage therapy and/or biocontrolling of S. flexneri in contaminated food and water.
Keywords: bacteriophage; Sf6; Shigella flexneri; serotype 2a; host range mutant; tailspike protein
Rights: © The Author(s) 2022. Published by Oxford University Press on behalf of FEMS. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited
DOI: 10.1093/femsle/fnac020
Grant ID: http://purl.org/au-research/grants/arc/DP170104325
Published version: http://dx.doi.org/10.1093/femsle/fnac020
Appears in Collections:Molecular and Biomedical Science publications

Files in This Item:
File Description SizeFormat 
hdl_134851.pdfPublished version1.82 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.