The inside scoop: Comparative genomics of two intranuclear bacteria, "Candidatus Berkiella cookevillensis" and "Candidatus Berkiella aquae".


Journal

PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081

Informations de publication

Date de publication:
2022
Historique:
received: 05 08 2022
accepted: 12 11 2022
entrez: 30 12 2022
pubmed: 31 12 2022
medline: 4 1 2023
Statut: epublish

Résumé

"Candidatus Berkiella cookevillensis" (strain CC99) and "Candidatus Berkiella aquae" (strain HT99), belonging to the Coxiellaceae family, are gram-negative bacteria isolated from amoebae in biofilms present in human-constructed water systems. Both bacteria are obligately intracellular, requiring host cells for growth and replication. The intracellular bacteria-containing vacuoles of both bacteria closely associate with or enter the nuclei of their host cells. In this study, we analyzed the genome sequences of CC99 and HT99 to better understand their biology and intracellular lifestyles. The CC99 genome has a size of 2.9Mb (37.9% GC) and contains 2,651 protein-encoding genes (PEGs) while the HT99 genome has a size of 3.6Mb (39.4% GC) and contains 3,238 PEGs. Both bacteria encode high proportions of hypothetical proteins (CC99: 46.5%; HT99: 51.3%). The central metabolic pathways of both bacteria appear largely intact. Genes for enzymes involved in the glycolytic pathway, the non-oxidative branch of the phosphate pathway, the tricarboxylic acid pathway, and the respiratory chain were present. Both bacteria, however, are missing genes for the synthesis of several amino acids, suggesting reliance on their host for amino acids and intermediates. Genes for type I and type IV (dot/icm) secretion systems as well as type IV pili were identified in both bacteria. Moreover, both bacteria contain genes encoding large numbers of putative effector proteins, including several with eukaryotic-like domains such as, ankyrin repeats, tetratricopeptide repeats, and leucine-rich repeats, characteristic of other intracellular bacteria.

Identifiants

pubmed: 36584052
doi: 10.1371/journal.pone.0278206
pii: PONE-D-22-22040
pmc: PMC9803151
doi:

Substances chimiques

Bacterial Proteins 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0278206

Subventions

Organisme : NIGMS NIH HHS
ID : R15 GM131357
Pays : United States

Informations de copyright

Copyright: © 2022 Kidane et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Destaalem T Kidane (DT)

Molecular Biosciences Program, Middle Tennessee State University, Murfreesboro, TN, United States of America.
Department of Biology, Middle Tennessee State University, Murfreesboro, TN, United States of America.

Yohannes T Mehari (YT)

Department of Biological Sciences, Auburn University, Auburn, AL, United States of America.

Forest C Rice (FC)

Department of Biology, Middle Tennessee State University, Murfreesboro, TN, United States of America.

Brock A Arivett (BA)

Division of Infectious Disease, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, United States of America.

John H Gunderson (JH)

Department of Biology, Tennessee Technological University, Cookeville, TN, United States of America.

Anthony L Farone (AL)

Molecular Biosciences Program, Middle Tennessee State University, Murfreesboro, TN, United States of America.
Department of Biology, Middle Tennessee State University, Murfreesboro, TN, United States of America.

Mary B Farone (MB)

Molecular Biosciences Program, Middle Tennessee State University, Murfreesboro, TN, United States of America.
Department of Biology, Middle Tennessee State University, Murfreesboro, TN, United States of America.

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