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CsrA-Controlled Proteins Reveal New Dimensions of Acinetobacter baumannii Desiccation Tolerance.
Oda, Yasuhiro; Shapiro, Madelyn M; Lewis, Nathan M; Zhong, Xuefei; Huse, Holly K; Zhong, Weizhi; Bruce, James E; Manoil, Colin; Harwood, Caroline S.
Afiliação
  • Oda Y; Department of Microbiology, University of Washingtongrid.34477.33, Seattle, Washington, USA.
  • Shapiro MM; Seattle Children's Research Institute, Center for Global Infectious Disease Research, Seattle, Washington, USA.
  • Lewis NM; Department of Plant and Microbial Biology, University of Minnesotagrid.17635.36, St. Paul, Minnesota, USA.
  • Zhong X; Analytical Chemistry Group, Regeneron Pharmaceuticals, Tarrytown, New York, USA.
  • Huse HK; Department of Pathology, Harbor-UCLA Medical Center, Torrance, California, USA.
  • Zhong W; Department of Microbiology, University of Washingtongrid.34477.33, Seattle, Washington, USA.
  • Bruce JE; Department of Genome Sciences, University of Washingtongrid.34477.33, Seattle, Washington, USA.
  • Manoil C; Department of Genome Sciences, University of Washingtongrid.34477.33, Seattle, Washington, USA.
  • Harwood CS; Department of Microbiology, University of Washingtongrid.34477.33, Seattle, Washington, USA.
J Bacteriol ; 204(4): e0047921, 2022 04 19.
Article em En | MEDLINE | ID: mdl-35285725
ABSTRACT
Hospital environments are excellent reservoirs for the opportunistic pathogen Acinetobacter baumannii in part because it is exceptionally tolerant to desiccation. We found that relative to other A. baumannii strains, the virulent strain AB5075 was strikingly desiccation resistant at 2% relative humidity (RH), suggesting that it is a good model for studies of the functional basis of this trait. Consistent with results from other A. baumannii strains at 40% RH, we found the global posttranscriptional regulator CsrA to be critically important for desiccation tolerance of AB5075 at 2% RH. Proteomics experiments identified proteins that were differentially present in wild-type and csrA mutant cells. Subsequent analysis of mutants in genes encoding some of these proteins revealed six genes that were required for wild-type levels of desiccation tolerance. These include genes for catalase, a universal stress protein, a hypothetical protein, and a biofilm-associated protein. Two genes of unknown function had very strong desiccation phenotypes, with one of the two genes predicting an intrinsically disordered protein (IDP) that binds to DNA. Intrinsically disordered proteins are widespread in eukaryotes but less so in prokaryotes. Our results suggest there are new mechanisms underlying desiccation tolerance in bacteria and identify several key functions involved. IMPORTANCE Acinetobacter baumannii is found in terrestrial environments but can cause nosocomial infections in very sick patients. A factor that contributes to the prevalence of A. baumannii in hospital settings is that it is intrinsically resistant to dry conditions. Here, we established the virulent strain A. baumannii AB5075 as a model for studies of desiccation tolerance at very low relative humidity. Our results show that this trait depends on two proteins of unknown function, one of which is predicted to be an intrinsically disordered protein. This category of protein is critical for the small animals named tardigrades to survive desiccation. Our results suggest that A. baumannii may have novel strategies to survive desiccation that have not previously been seen in bacteria.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Acinetobacter baumannii / Proteínas Intrinsicamente Desordenadas Tipo de estudo: Prognostic_studies / Risk_factors_studies Limite: Animals / Humans Idioma: En Revista: J Bacteriol Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Acinetobacter baumannii / Proteínas Intrinsicamente Desordenadas Tipo de estudo: Prognostic_studies / Risk_factors_studies Limite: Animals / Humans Idioma: En Revista: J Bacteriol Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos