VgrG and PAAR Proteins Define Distinct Versions of a Functional Type VI Secretion System
Proteomics
0301 basic medicine
570
QH301-705.5
Immunoblotting
610
RC581-607
Type VI Secretion Systems
Chromatography, Affinity
Coculture Techniques
Mass Spectrometry
03 medical and health sciences
Bacterial Proteins
Escherichia coli
Amino Acid Sequence
Immunologic diseases. Allergy
Biology (General)
Serratia marcescens
Research Article
DOI:
10.1371/journal.ppat.1005735
Publication Date:
2016-06-28T13:40:55Z
AUTHORS (6)
ABSTRACT
The Type VI secretion system (T6SS) is widespread among bacterial pathogens and acts as an effective weapon against competitor bacteria eukaryotic hosts by delivering toxic effector proteins directly into target cells. T6SS utilises a bacteriophage-like contractile machinery to expel puncturing device based on tube of Hcp topped with VgrG spike, which can be extended final tip from PAAR domain-containing protein. Effector are believed delivered specifically associating particular Hcp, or proteins, either covalently ('specialised') non-covalently ('cargo' effectors). Here we used the opportunistic pathogen Serratia marcescens, together integratecd genetic, proteomic biochemical approaches, elucidate role specific homologues in function specificity, revealing new aspects unexpected subtleties delivery T6SS. We identified effectors, both cargo specialised, absolutely dependent for cells, discovered that other effectors show preference VgrG. presence at least one protein was found essential function, consistent designation 'core' component. showed VgrG-PAAR combinations required assemble functional three distinct assemblies S. marcescens exhibit specificity efficiency. Unexpectedly, two different PAAR-containing Rhs functionally pair same Showing accessory EagR involved these interactions, native VgrG-Rhs-EagR complexes were isolated interactions between cognate identified. This study defines yet flexible highlights existence versions differential efficiency cell delivery.
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