An Unprecedented Tolerance to Deletion of the Periplasmic Chaperones SurA, Skp, and DegP in the Nosocomial Pathogen Acinetobacter baumannii-Reference-Cited by-同舟云学术

An Unprecedented Tolerance to Deletion of the Periplasmic Chaperones SurA, Skp, and DegP in the Nosocomial Pathogen Acinetobacter baumannii

Published:2022-10-18 Issue:10 Volume:204 Page:
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Birkle Karolin¹,Renschler Fabian¹,Angelov Angel¹²,Wilharm Gottfried³^ORCID,Franz-Wachtel Mirita⁴,Maček Boris⁴,Bohn Erwin¹,Weber Elena¹,Müller Jennifer²,Friedrich Lea¹,Schütz Monika¹⁵^ORCID

Affiliation:

1. Institut für Medizinische Mikrobiologie und Hygiene, Tübingen, Germany

2. NGS Competence Center Tübingen (NCCT), Tübingen, Germany

3. Robert Koch-Institute, Wernigerode Branch, Wernigerode, Germany

4. Proteome Center Tübingen, Universität Tübingen, Tübingen, Germany

5. German Center for Infection Research (DZIF), partner site Tübingen, Tübingen, Germany

Abstract

Acinetobacter baumannii is a major threat to human health due to its ability to persist in the hospital environment, resistance to antibiotic treatment, and ability to deploy multiple and redundant virulence factors. In a rising number of cases, infections with multidrug-resistant A. baumannii end up fatally, because all antibiotic treatment options fail.

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.00054-22

Reference72 articles.

1. Molecular Basis of Bacterial Outer Membrane Permeability Revisited

2. Outer membrane permeability and antibiotic resistance

3. Folding mechanisms of periplasmic proteins

4. The β-barrel assembly machinery in motion

5. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.

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