Evidence map›Paper›PMID 36451021›Full record

ArticleCommunications biology2022

In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.

Luis F Avila-Cobian, Stefania De Benedetti, Choon Kim, Rhona Feltzer, Matthew M Champion, Jed F Fisher, Shahriar Mobashery

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Luis F Avila-CobianDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Stefania De BenedettiDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.ORCID 0000-0001-9284-9623
Choon KimDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.ORCID 0000-0003-0306-8935
Rhona FeltzerDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.ORCID 0000-0002-2071-1323
Matthew M ChampionDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Jed F FisherDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA. mobashery@nd.edu.ORCID 0000-0002-7695-7883
University of Notre Dame · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
Cell-Wall Recycling and Nexus to Antibiotic ResistanceR35GM131685 · NIGMS · UNIVERSITY OF NOTRE DAME · PI MOBASHERY, SHAHRIAR · 2019 to 2023
$1.9M
NIGMS NIH HHS R35 GM131685NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

The protein networks of cell-wall-biosynthesis assemblies are largely unknown. A key class of enzymes in these assemblies is the lytic transglycosylases (LTs), of which eleven exist in P. aeruginosa. We have undertaken a pulldown strategy in conjunction with mass-spectrometry-based proteomics to identify the putative binding partners for the eleven LTs of P. aeruginosa. A total of 71 putative binding partners were identified for the eleven LTs. A systematic assessment of the binding partners of the rare lipoprotein A (RlpA), one of the pseudomonal LTs, was made. This 37-kDa lipoprotein is involved in bacterial daughter-cell separation by an unknown process. RlpA participates in both the multi-protein and multi-enzyme divisome and elongasome assemblies. We reveal an extensive protein-interaction network for RlpA involving at least 19 proteins. Their kinetic parameters for interaction with RlpA were assessed by microscale thermophoresis, surface-plasmon resonance, and isothermal-titration calorimetry. Notable RlpA binding partners include PBP1b, PBP4, and SltB1. Elucidation of the protein-interaction networks for each of the LTs, and specifically for RlpA, opens opportunities for the study of their roles in the complex protein assemblies intimately involved with the cell wall as a structural edifice critical for bacterial survival.

Indexed as

Lipoprotein(a)Pseudomonas aeruginosaCell WallGlycosyltransferasesProtein Interaction MapsGlycosyltransferasesLipoprotein(a)

Identifiers

PMID36451021
PMCPMC9712689
OpenAlexW4310641794

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.