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Convergent evolution of plant pattern recognition receptors sensing cysteine-rich patterns from three microbial kingdoms

ABSTRACT: Plants deploy pattern recognition receptors to detect microbe- and damage-associated molecular patterns. Arabidopsis thaliana receptor-like protein RLP30 contributes to innate immunity to the necrotrophic fungus Sclerotinia sclerotiorum by recognizing SCLEROTINIA CULTURE FILTRATE ELICITOR 1 (SCFE1). Here we show that the S. sclerotiorum small cysteine-rich protein SCP1 accounts for elicitor activity of SCFE1. RLP30 recognizes SCP1 and its homologs from divergent fungi and oomycetes, as well as an SCP1-unrelated and conserved pattern from bacterial Pseudomonads. Stable expression of RLP30 in Nicotiana tabacum confers enhanced immunity to bacterial, fungal, and oomycete pathogens. Unlike Arabidopsis, which requires intact SCP1 for RLP30-mediated immunity, other Brassicaceae and Solanaceae respond to smaller immunogenic SCP1 epitopes. We conclude that Arabidopsis RLP30 recognizes immunogenic patterns from three microbial kingdoms and that mechanistically different SCP1 perception has evolved in other plant species, likely as a result of convergent evolution.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Sclerotinia Sclerotiorum

SUBMITTER: Christina Ludwig

LAB HEAD: Christina Ludwig

PROVIDER: PXD036013 | Pride | 2023-06-14

REPOSITORIES: Pride

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			Action	DRS
	BBM_080_P053_02_HEK_002.raw	Raw
	BBM_080_P053_02_HEK_003.raw	Raw
	BBM_080_P053_02_HEK_004.raw	Raw
	BBM_080_P053_02_HEK_005.raw	Raw
	BBM_080_P053_02_HEK_006.raw	Raw

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Project description:Detection of immunogenic proteins remains an important task for life sciences as it nourishes the understanding of pathogenicity, illuminates new potential vaccine candidates and broadens the spectrum of biomarkers applicable in diagnostic tools. Traditionally, immunoscreenings of expression libraries via polyclonal sera on nitrocellulose membranes or screenings of whole proteome lysates in 2-D gel electrophoresis are performed. However, these methods feature some rather inconvenient disadvantages. Screening of expression libraries to expose novel antigens from bacteria often lead to an abundance of false positive signals owing to the high cross reactivity of polyclonal antibodies towards the proteins of the expression host. A method is presented that overcomes many disadvantages of the old procedures. We incorporated a fusion tag prior to our genes of interest and attached the expressed fusion proteins covalently on microarrays. This enhances the specific binding of the proteins compared to nitrocellulose. Thus, it helps to reduce the number of false positives significantly. It enables us to screen for immunogenic proteins in a shorter time, with more samples and statistical reliability. We validated our method by employing several known genes from Campylobacter jejuni NCTC 11168. Four of proteins that have previously been described as immunogenic have successfully been assessed immunogenic abilities with our method. One protein with no known immunogenic behaviour before suggested potential immunogenicity. The method presented offers a new approach for screening of bacterial expression libraries to illuminate novel proteins with immunogenic features. It could provide a powerful and attractive alternative to existing methods and help to detect and identify bacterial virulence factors, vaccine candidates and potential biomarkers. The overall study was done with five technical replicates. Ten proteins derived from Campylobacter jejuni were tested regarding their immunogenic potential. The ten proteins derived from Campylobacter jejuni were fusion proteins, i.e., N-terminal HaloTag fused to: Gene <--> Protein cjaA <--> putative amino-acid transporter periplasmic solute-binding protein hisJ <--> histidine-binding protein precursor pal <--> peptidoglycan associated lipoprotein flaC <--> flagellin flaA <--> flagellin peb1a <--> bifunctional adhesin/ABC transporter aspartate/glutamate-binding protein pyrC <--> dihydroorotase (EC:3.5.2.3) pseB <--> UDP-GlcNAc-specific C4,6 dehydratase/C5 epimerase gapA <--> glyceraldehyde 3-phosphate dehydrogenase (EC:1.2.1.12) argC <--> N-acetyl-gamma-glutamyl-phosphate reductase (EC:1.2.1.38)

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Convergent evolution of plant pattern recognition receptors sensing cysteine-rich patterns from three microbial kingdoms

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