Paper · 2018 · Frontiers in Plant Science

Development of a Rapid in planta BioID System as a Probe for Plasma Membrane-Associated Immunity Proteins

Brendon Conlan; Thomas Stoll; Jeffrey J. Gorman; et al.

6
claims
12
verbatim quotes
53
citations
3
research areas
✓
Open access · cc-by

Abstract

Plant pathogens secrete effector molecules that suppress the plant immune response to facilitate disease development. AvrPto is a well-studied effector from the phytopathogenic bacterium Pseudomonas syringae. Here we utilise an in planta proximity dependent biotin ligase labelling technique (BioID) in combination with AvrPto to identify proximal proteins that are potential immune system components. The labelling technique biotinylated proteins proximal to AvrPto at the plasma-membrane allowing their isolation and identification by mass spectrometry. Five AvrPto proximal plant proteins (APPs) were identified and their effect on plant immune function and growth was examined in Nicotiana benthamiana leaves. One protein identified, RIN4, is a central immune component previously shown to interact with AvrPto. Two other proteins were identified which form a complex and when silenced significantly reduced Pseudomonas syringe tabaci growth. The first was a receptor like protein kinase (APK1) which was required for Pto/Prf signalling and the second was Target of Myb1 (TOM1), a membrane associated protein with a phosphatidylinositol 5-phosphate (PtdIns5P) binding motif. We have developed a technology to rapidly determine protein interactions within living plant tissue. It is particularly useful for identifying plant immune system components by defining pathogenic effector protein interactions within their plant hosts.

Abstract from the paper’s OpenAlex record; open copy licensed cc-by. Read at the source ↗

The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.

Claims 6

Method / resourceobservedoriginal resultpositivemeasured

Claim · model-written summary

BioID labelled proteins near AvrPto at the plasma membrane for mass spectrometry identification.

Taxon
Nicotiana benthamianaNicotiana benthamianae1
Outcome
biotinylated proteins proximal to AvrPtoe0

Not reportedComparatorValue

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“The labelling technique biotinylated proteins proximal to AvrPto at the plasma-membrane allowing their isolation and identification by mass spectrometry”

✓ located verbatim in the source · abstract, characters 402–554 · show in text ↑
e1

“Nicotiana benthamiana leaves”

✓ located verbatim in the source · abstract, characters 684–712 · show in text ↑
Method / resourceobservedoriginal resultpositivemeasured

Claim · model-written summary

Five plant proteins proximal to AvrPto were identified.

Taxon
Nicotiana benthamianaNicotiana benthamianae1
Outcome
AvrPto proximal plant proteinse0
Value
Fivee0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“Five AvrPto proximal plant proteins (APPs) were identified”

✓ located verbatim in the source · abstract, characters 556–614 · show in text ↑
e1

“Nicotiana benthamiana leaves”

✓ located verbatim in the source · abstract, characters 684–712 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

RIN4 was identified among the AvrPto proximal proteins.

Taxon
Nicotiana benthamianaNicotiana benthamianae1
Gene
RIN4e0
Outcome
One protein identified, RIN4e0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“One protein identified, RIN4, is a central immune component previously shown to interact with AvrPto”

✓ located verbatim in the source · abstract, characters 714–814 · show in text ↑
e1

“Nicotiana benthamiana leaves”

✓ located verbatim in the source · abstract, characters 684–712 · show in text ↑
Intervention effectobservedoriginal resultpositivesignificant (as stated)measured

Claim · model-written summary

Silencing two proteins that form a complex significantly reduced Pseudomonas syringe tabaci growth.

Taxon
Nicotiana benthamianaNicotiana benthamianae1
Treatment
silencede0
Interactor
Pseudomonas syringe tabacie0pathogen
Outcome
Pseudomonas syringe tabaci growthe0
Direction
reducede0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“Two other proteins were identified which form a complex and when silenced significantly reduced Pseudomonas syringe tabaci growth”

✓ located verbatim in the source · abstract, characters 816–945 · show in text ↑
e1

“Nicotiana benthamiana leaves”

✓ located verbatim in the source · abstract, characters 684–712 · show in text ↑
Mechanismobservedoriginal resultmeasured

Claim · model-written summary

APK1 was required for Pto/Prf signalling.

Taxon
Nicotiana benthamianaNicotiana benthamianae1
Gene
APK1e0
Outcome
Pto/Prf signallinge0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“a receptor like protein kinase (APK1) which was required for Pto/Prf signalling”

✓ located verbatim in the source · abstract, characters 961–1040 · show in text ↑
e1

“Nicotiana benthamiana leaves”

✓ located verbatim in the source · abstract, characters 684–712 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

TOM1 was identified as a membrane protein with a PtdIns5P binding motif.

Taxon
Nicotiana benthamianaNicotiana benthamianae1
Gene
Target of Myb1 (TOM1)e0
Outcome
a membrane associated protein with a phosphatidylinositol 5-phosphate (PtdIns5P) binding motife0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“Target of Myb1 (TOM1), a membrane associated protein with a phosphatidylinositol 5-phosphate (PtdIns5P) binding motif”

✓ located verbatim in the source · abstract, characters 1060–1177 · show in text ↑
e1

“Nicotiana benthamiana leaves”

✓ located verbatim in the source · abstract, characters 684–712 · show in text ↑

loss of function · growth · Nicotiana benthamianaPositive and negative results

21 papers: 4 positive, 17 negative or no effect

3 papers in the same direction as this paper · 17 in the opposite direction

  1. negative
  2. negative
  3. no effect

17 papers more in this group

See all 21 papers →

Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.