Evidence map›Paper›PMID 34398935›Full record

ArticlePLoS pathogens2021

The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.

Edgar E Llontop, William Cenens, Denize C Favaro, Germán G Sgro, Roberto K Salinas, Cristiane R Guzzo, Chuck S Farah

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

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  15. Genomic and phenotypic insight intoFrontiers in microbiology · 2023
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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.

Edgar E LlontopDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0003-4910-9667
William CenensDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0002-0856-4703
Denize C FavaroDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0001-5563-2548
Germán G SgroDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0002-2831-7945
Roberto K SalinasDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0003-1032-7683
Cristiane R GuzzoDepartamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0002-5664-8055
Chuck S FarahDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0003-3110-6302
Universidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria that undergo cycles of extension and retraction and participate in a variety of important functions related to lifestyle, defense and pathogenesis. During pilus extensions, the PilB ATPase energizes the polymerization of pilin monomers from the inner membrane. In Xanthomonas citri, two cytosolic proteins, PilZ and the c-di-GMP receptor FimX, are involved in the regulation of T4P biogenesis through interactions with PilB. In vivo fluorescence microscopy studies show that PilB, PilZ and FimX all colocalize to the leading poles of X. citri cells during twitching motility and that this colocalization is dependent on the presence of all three proteins. We demonstrate that full-length PilB, PilZ and FimX can interact to form a stable complex as can PilB N-terminal, PilZ and FimX C-terminal fragments. We present the crystal structures of two binary complexes: i) that of the PilB N-terminal domain, encompassing sub-domains ND0 and ND1, bound to PilZ and ii) PilZ bound to the FimX EAL domain within a larger fragment containing both GGDEF and EAL domains. Evaluation of PilZ interactions with PilB and the FimX EAL domain in these and previously published structures, in conjunction with mutagenesis studies and functional assays, allow us to propose an internally consistent model for the PilB-PilZ-FimX complex and its interactions with the PilM-PilN complex in the context of the inner membrane platform of the X. citri Type IV pilus.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCrystallography, X-RayFimbriae, BacterialOxidoreductasesProtein BindingProtein ConformationProtein Interaction Domains and MotifsVirulenceXanthomonasAdenosine TriphosphatasesBacterial ProteinsOxidoreductasespilB protein, Bacteria

Identifiers

PMID34398935
PMCPMC8389850
OpenAlexW3196123584

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.