Identification of MAMP-Responsive Plasma Membrane-Associated Proteins in Arabidopsis thaliana Following Challenge with Different LPS Chemotypes from Xanthomonas campestris.

Lizelle A. Piater,Raeesa H. Hussan,Ian A. Dubery

doi:10.3390/pathogens9100787

Lizelle A. Piater, Raeesa H. Hussan + Show 1 more

Open Access

https://doi.org/10.3390/pathogens9100787

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Journal: Pathogens (Basel, Switzerland)	Publication Date: Sep 25, 2020
Citations: 14	License type: CC BY 4.0

Affiliation: University of Johannesburg

Abstract

Lipopolysaccharides (LPS) are recognized as microbe-associated molecular patterns (MAMPs) responsible for eliciting defense-related responses and while the effects have been well-documented in mammals, there is a lack of knowledge regarding the mechanism of perception in plant systems and recognized structural moieties within the macromolecular lipoglycan structure. Thus, identification of the LPS plasma membrane (PM) receptor(s)/receptor complex in Arabidopsis thaliana through proteomics will contribute to a deeper understanding of induced defense responses. As such, structurally characterized LPS chemotypes from Xanthomonas campestris pv. campestris (Xcc) wild-type 8004 (prototypical smooth-type LPS) and mutant 8530 (truncated core with no O–chain) strains were utilized to pre-treat A. thaliana plants. The associated proteomic response/changes within the PM were compared over a 24 h period using mass spectrometry-based methodologies following three variants of LPS-immobilized affinity chromatography. This resulted in the identification of proteins from several functional categories, but importantly, those involved in perception and defense. The distinct structural features between wild-type and mutant LPS are likely responsible for the differential changes to the proteome profiles, and many of the significant proteins were identified in response to the wild-type Xcc LPS where it is suggested that the core oligosaccharide and O-chain participate in recognition by receptor-like kinases (RLKs) in a multiprotein complex and, notably, varied from that of the mutant chemotype.

Highlights

Pathogenic microbes affect a plant’s development, reproduction, and production yield [1] and as such, the control thereof remains a major challenge in agriculture
The distinct structural features between wild-type and mutant LPS are likely responsible for the differential changes to the proteome profiles, and many of the significant proteins were identified in response to the wild-type Xanthomonas campestris pv. campestris (Xcc) LPS where it is suggested that the core oligosaccharide and O-chain participate in recognition by receptor-like kinases (RLKs) in a multiprotein complex and, notably, varied from that of the mutant chemotype
On the LPSB. cepacia -interacting proteins in A. thaliana suggests that the perception of the lipoglycan could possibly occur within membrane rafts/microdomains

Summary

Introduction

Pathogenic microbes affect a plant’s development, reproduction, and production yield [1] and as such, the control thereof remains a major challenge in agriculture. One such pathogen is the Gram-negative Xanthomonas campestris pv. Gram-negative bacteria, lipopolysaccharides (LPS) are found in the outer membrane [3]. LPS to the outer membrane [4,5]. LPS plays an important role in cell viability, host attachment, and bacterial virulence and activates an immune response in both mammals and plants [3]. The recognition and LPS-induced signaling in mammalian cells have been well documented and involves interaction of the lipid A moiety, which forms a complex with the LPS-binding protein (LBP), CD14 receptor, Toll-like receptor 4 (TLR4)-myeloid differentiation protein 2 (MD2), and caspase-4/11

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