The C. elegans CHP1 homolog, pbo-1, functions in innate immunity by regulating the pH of the intestinal lumen.


Journal

PLoS pathogens
ISSN: 1553-7374
Titre abrégé: PLoS Pathog
Pays: United States
ID NLM: 101238921

Informations de publication

Date de publication:
01 2020
Historique:
received: 25 09 2018
accepted: 07 10 2019
entrez: 10 1 2020
pubmed: 10 1 2020
medline: 28 4 2020
Statut: epublish

Résumé

Caenorhabditis elegans are soil-dwelling nematodes and models for understanding innate immunity and infection. Previously, we developed a novel fluorescent dye (KR35) that accumulates in the intestine of C. elegans and reports a dynamic wave in intestinal pH associated with the defecation motor program. Here, we use KR35 to show that mutations in the Ca2+-binding protein, PBO-1, abrogate the pH wave, causing the anterior intestine to be constantly acidic. Surprisingly, pbo-1 mutants were also more susceptible to infection by several bacterial pathogens. We could suppress pathogen susceptibility in pbo-1 mutants by treating the animals with pH-buffering bicarbonate, suggesting the pathogen susceptibility is a function of the acidity of the intestinal pH. Furthermore, we use KR35 to show that upon infection by pathogens, the intestinal pH becomes neutral in a wild type, but less so in pbo-1 mutants. C. elegans is known to increase production of reactive oxygen species (ROS), such as H2O2, in response to pathogens, which is an important component of pathogen defense. We show that pbo-1 mutants exhibited decreased H2O2 in response to pathogens, which could also be partially restored in pbo-1 animals treated with bicarbonate. Ultimately, our results support a model whereby PBO-1 functions during infection to facilitate pH changes in the intestine that are protective to the host.

Identifiants

pubmed: 31917826
doi: 10.1371/journal.ppat.1008134
pii: PPATHOGENS-D-18-01864
pmc: PMC6952083
doi:

Substances chimiques

Bicarbonates 0
Caenorhabditis elegans Proteins 0
PBO-1 protein, C elegans 0
Calcineurin EC 3.1.3.16

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

e1008134

Subventions

Organisme : NIGMS NIH HHS
ID : P20 GM113117
Pays : United States
Organisme : NIGMS NIH HHS
ID : P20 GM103418
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM133572
Pays : United States
Organisme : NIGMS NIH HHS
ID : P20 GM103638
Pays : United States
Organisme : NIGMS NIH HHS
ID : K12 GM063651
Pays : United States

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Saida Benomar (S)

Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, United States of America.

Patrick Lansdon (P)

Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, United States of America.

Aaron M Bender (AM)

Department of Medicinal Chemistry, The University of Kansas, Lawrence, KS, United States of America.

Blake R Peterson (BR)

Department of Medicinal Chemistry, The University of Kansas, Lawrence, KS, United States of America.

Josephine R Chandler (JR)

Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, United States of America.

Brian D Ackley (BD)

Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, United States of America.

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