A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPα) conjugative machineries and their cognate Escherichia coli host strains

SynopsisKlebsiella-associated plasmid pKpQIL and its variant have been isolated globally. Our study aimed to determine whether a naturally occurring variant has altered host range and impacts on the fitness of different bacterial host strains. The plasmids pKpQIL-UK and pKpQIL-D2 were transferred from the original clinical isolate host strains of Klebsiella pneumoniae into Escherichia coli, Salmonella Typhimurium, Enterobacter cloacae and Serratia marcescens strains by filter-mating and conjugation frequencies determined and compared. The fitness of the resulting transconjugants was assessed by determining growth kinetics, ability to form a biofilm and persistence of the plasmids in each host was also measured. Transfer of either plasmid into Salmonella and S. marcescens was similar. However, pKpQIL-UK transferred into E. coli at a higher rate than did pKpQIL-D2; the reverse was found for E. cloacae. Both plasmids were rapidly lost from the E. coli population. Plasmid pKpQIL-UK, but not -D2, was able to persist in Salmonella. Although pKpQIL-UK imposed a greater fitness cost (inferred from an increased generation time) than -D2 on E. cloacae, it was able to persist as well as pKpQIL-D2 in this host. The pKpQIL-D2 plasmid did not confer any fitness benefit on any of the hosts under the conditions tested. Variants of the globally important pKpQIL plasmid have arisen in patients due to recombination. The impacts of the pKpQIL-UK plasmid and the -D2 variant in various Enterobacteriaceae are host-dependent. Continuing evolution of pKpQIL may alter its host range in the future.

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Conjugal transfer of broad-host-range incompatibility group P and Q plasmids from Escherichia coli to Actinobacillus actinomycetemcomitans.

Infection and Immunity ◽

10.1128/iai.61.8.3544-3547.1993 ◽

1993 ◽

Vol 61 (8) ◽

pp. 3544-3547 ◽

Cited By ~ 23

Author(s):

P Goncharoff ◽

J K Yip ◽

H Wang ◽

H C Schreiner ◽

J A Pai ◽

...

Keyword(s):

Escherichia Coli ◽

Host Range ◽

Conjugal Transfer ◽

Actinobacillus Actinomycetemcomitans ◽

Broad Host Range ◽

Incompatibility Group

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Bio-control of O157:H7, and colistin-resistant MCR-1-positive Escherichia coli using a new designed broad host range phage cocktail

LWT ◽

10.1016/j.lwt.2021.112836 ◽

2021 ◽

pp. 112836

Author(s):

Khashayar Shahin ◽

Hongduo Bao ◽

Shujiao Zhu ◽

Abbas Soleimani-Delfan ◽

Tao He ◽

...

Keyword(s):

Escherichia Coli ◽

Host Range ◽

Broad Host Range ◽

Phage Cocktail

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LamB, OmpC, and the Core Lipopolysaccharide of Escherichia coli K-12 Function as Receptors of Bacteriophage Bp7

Journal of Virology ◽

10.1128/jvi.00325-20 ◽

2020 ◽

Vol 94 (12) ◽

Cited By ~ 1

Author(s):

Peipei Chen ◽

Huzhi Sun ◽

Huiying Ren ◽

Wenhua Liu ◽

Guimei Li ◽

...

Keyword(s):

Escherichia Coli ◽

Host Range ◽

Inner Core ◽

Phage Infection ◽

Broad Host Range ◽

Content Type ◽

E Coli ◽

Phage Adsorption ◽

Specific Receptors ◽

K 12

ABSTRACT Bp7 is a T-even phage with a broad host range specific to Escherichia coli, including E. coli K-12. The receptor binding protein (RBP) of bacteriophages plays an important role in the phage adsorption process and determines phage host range, but the molecular mechanism involved in host recognition of phage Bp7 remains unknown. In this study, the interaction between phage Bp7 and E. coli K-12 was investigated. Based on homology alignment, amino acid sequence analysis, and a competitive assay, gp38, located at the tip of the long tail fiber, was identified as the RBP of phage Bp7. Using a combination of in vivo and in vitro approaches, including affinity chromatography, gene knockout mutagenesis, a phage plaque assay, and phage adsorption kinetics analysis, we identified the LamB and OmpC proteins on the surface of E. coli K-12 as specific receptors involved in the first step of reversible phage adsorption. Genomic analysis of the phage-resistant mutant strain E. coli K-12-R and complementation tests indicated that HepI of the inner core of polysaccharide acts as the second receptor recognized by phage Bp7 and is essential for successful phage infection. This observation provides an explanation of the broad host range of phage Bp7 and provides insight into phage-host interactions. IMPORTANCE The RBPs of T4-like phages are gp37 and gp38. The interaction between phage T4 RBP gp37 and its receptors has been clarified by many reports. However, the interaction between gp38 and its receptors during phage adsorption is still not completely understood. Here, we identified phage Bp7, which uses gp38 as an RBP, and provided a good model to study the phage-host interaction mechanisms in an enterobacteriophage. Our study revealed that gp38 of phage Bp7 recognizes the outer membrane proteins (OMPs) LamB and OmpC of E. coli K-12 as specific receptors and binds with them reversibly. HepI of the inner-core oligosaccharide is the second receptor and binds with phage Bp7 irreversibly to begin the infection process. Determining the interaction between the phage and its receptors will help elucidate the mechanisms of phage with a broad host range and help increase understanding of the phage infection mechanism based on gp38.

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