Evidence map›Paper›PMID 25343965›Full record

ArticleBMC microbiology2014

A systematic analysis of the in vitro and in vivo functions of the HD-GYP domain proteins of Vibrio cholerae.

Robert W McKee, Ankunda Kariisa, Benjamin Mudrak, Courtney Whitaker, Rita Tamayo

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026
    Article
  5. Review
  6. A comparative genomic and phenotypic study ofMicrobiology (Reading, England) · 2024
    Article
  7. Biochemistry · 2022
    Article
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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

5 authors at 1 institution in 1 country.

Robert W McKeeDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, 125 Mason Farm Rd, CB# 7290, Chapel Hill, NC, USA. robert_mckee@med.unc.edu.
Ankunda KariisaDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, 125 Mason Farm Rd, CB# 7290, Chapel Hill, NC, USA. akariisa@gmail.com.
Benjamin MudrakDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, 125 Mason Farm Rd, CB# 7290, Chapel Hill, NC, USA. benmudrak@gmail.com.
Courtney WhitakerDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, 125 Mason Farm Rd, CB# 7290, Chapel Hill, NC, USA. cmwhitak@live.unc.edu.
Rita TamayoDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, 125 Mason Farm Rd, CB# 7290, Chapel Hill, NC, USA. rtamayo@med.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe second messenger cyclic diguanylate (c-di-GMP) plays a central role in bacterial adaptation to extracellular stimuli, controlling processes such as motility, biofilm development, cell development and, in some pathogens, virulence. The intracellular level of c-di-GMP is controlled by the complementary activities of diguanylate cyclases containing a GGDEF domain and two classes of c-di-GMP phosphodiesterases containing an EAL or HD-GYP hydrolytic domain. Compared to the GGDEF and EAL domains, the functions of HD-GYP domain family proteins are poorly characterized. The human diarrheal pathogen Vibrio cholerae encodes nine putative HD-GYP domain proteins. To determine the contributions of HD-GYP domain proteins to c-di-GMP signaling in V. cholerae, we systematically analyzed the enzymatic functionality of each protein and their involvement in processes known to be regulated by c-di-GMP: motility, biofilm development and virulence.

resultsComplementary in vitro and in vivo experiments showed that four HD-GYP domain proteins are active c-di-GMP phosphodiesterases: VC1295, VC1348, VCA0210 and VCA0681. Mutation of individual HD-GYP domain genes, as well as combinatorial mutations of multiple HD-GYP domain genes, had no effect on motility or biofilm formation of V. cholerae under the conditions tested. Furthermore, no single HD-GYP domain gene affected intestinal colonization by V. cholerae in an infant mouse model. However, inactivation of multiple HD-GYP domain genes, including the four encoding functional phosphodiesterases, significantly attenuated colonization.

conclusionsThese results indicate that the HD-GYP family of c-di-GMP phosphodiesterases impacts signaling by this second messenger during infection. Altogether, this work greatly furthers the understanding of this important family of c-di-GMP metabolic enzymes and demonstrates a role for HD-GYP domain proteins in the virulence of V. cholerae.

Indexed as

Signal Transduction3',5'-Cyclic-GMP PhosphodiesterasesAnimalsBiofilmsCholeraCyclic GMPDisease Models, AnimalLocomotionMiceMutationVibrio choleraeVirulence3',5'-Cyclic-GMP Phosphodiesterasesbis(3',5')-cyclic diguanylic acidCyclic GMP

Identifiers

PMID25343965
PMCPMC4212101
OpenAlexW2005487829

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.