Skip to content
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
immunology and microbiology
Pore-forming pyocin S5 utilizes the FptA ferripyochelin receptor to kill Pseudomonas aeruginosa
Microbiology (United Kingdom), Volume 160, No. PART 2, Year 2014
Notification
URL copied to clipboard!
Description
Pyocins are toxic proteins produced by some strains of Pseudomonas aeruginosa that are lethal for related strains of the same species. Some soluble pyocins (S2, S3 and S4) were previously shown to use the pyoverdine siderophore receptors to enter the cell. The P. aeruginosa PAO1 pore-forming pyocin S5 encoding gene (PAO985) was cloned into the expression vector pET15b, and the affinity-purified protein product tested for its killing activity against different P. aeruginosa strains. The results, however, did not show any correlation with a specific ferripyoverdine receptor. To further identify the S5 receptor, transposon mutants were generated. Pooled mutants were exposed to pyocin S5 and the resistant colonies growing in the killing zone were selected. The majority of S5-resistant mutants had an insertion in the fptA gene encoding the receptor for the siderophore pyochelin. Complementation of an fptA transposon mutant with the P. aeruginosa fptA gene in trans restored the sensitivity to S5. In order to define the receptor-binding domain of pyocin S5, two hybrid pyocins were constructed containing different regions from pyocin S5 fused to the C-terminal translocation and DNase killing domains of pyocin S2. Only the protein containing amino acid residues 151 to 300 from S5 showed toxicity, indicating that the pyocin S5 receptor-binding domain is not at the N-terminus of the protein as in other S-type pyocins. Pyocin S5 was, however, unable to kill Burkholderia cenocepacia strains producing a ferripyochelin FptA receptor, nor was the B. cenocepacia fptA gene able to restore the sensitivity of the resistant fptA mutant P. aeruginosa strain. © 2014 SGM.
Authors & Co-Authors
Elfarash, Ameer
Belgium, Brussels
Vrije Universiteit Brussel
Egypt, Asyut
Assiut University
Dingemans, Jozef
Belgium, Brussels
Vrije Universiteit Brussel
Ye, Lumeng
Belgium, Brussels
Vrije Universiteit Brussel
Hassan, Ahmed Amir
Belgium, Brussels
Vrije Universiteit Brussel
Craggs, Michael
Belgium, Brussels
Vrije Universiteit Brussel
Reimmann, Cornelia
Switzerland, Lausanne
Université de Lausanne Unil
Thomas, Mark S.
United Kingdom, Sheffield
The University of Sheffield
Cornelis, Pierre
Belgium, Brussels
Vrije Universiteit Brussel
Statistics
Citations: 50
Authors: 8
Affiliations: 4
Identifiers
Doi:
10.1099/mic.0.070672-0
ISSN:
13500872
Research Areas
Environmental
Genetics And Genomics