دورية أكاديمية
أعرض في EDS

Time-Resolved Proteome Analysis of Listeria monocytogenes during Infection Reveals the Role of the AAA+ Chaperone ClpC for Host Cell Adaptation.

التفاصيل البيبلوغرافية
العنوان: Time-Resolved Proteome Analysis of Listeria monocytogenes during Infection Reveals the Role of the AAA+ Chaperone ClpC for Host Cell Adaptation.
المؤلفون: Birk MS; Max Planck Unit for the Science of Pathogens, Berlin, Germany., Ahmed-Begrich R; Max Planck Unit for the Science of Pathogens, Berlin, Germany., Tran S; Max Planck Unit for the Science of Pathogens, Berlin, Germany., Elsholz AKW; Max Planck Unit for the Science of Pathogens, Berlin, Germany., Frese CK; Max Planck Unit for the Science of Pathogens, Berlin, Germany., Charpentier E; Max Planck Unit for the Science of Pathogens, Berlin, Germany.
المصدر: MSystems [mSystems] 2021 Aug 31; Vol. 6 (4), pp. e0021521. Date of Electronic Publication: 2021 Aug 03.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 101680636 Publication Model: Print-Electronic Cited Medium: Print ISSN: 2379-5077 (Print) Linking ISSN: 23795077 NLM ISO Abbreviation: mSystems Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Society for Microbiology, [2016]-
مستخلص: The cellular proteome comprises all proteins expressed at a given time and defines an organism's phenotype under specific growth conditions. The proteome is shaped and remodeled by both protein synthesis and protein degradation. Here, we developed a new method which combines metabolic and chemical isobaric peptide labeling to simultaneously determine the time-resolved protein decay and de novo synthesis in an intracellular human pathogen. We showcase this method by investigating the Listeria monocytogenes proteome in the presence and absence of the AAA+ chaperone protein ClpC. ClpC associates with the peptidase ClpP to form an ATP-dependent protease complex and has been shown to play a role in virulence development in L. monocytogenes. However, the mechanism by which ClpC is involved in the survival and proliferation of intracellular L. monocytogenes remains elusive. Employing this new method, we observed extensive proteome remodeling in L. monocytogenes upon interaction with the host, supporting the hypothesis that ClpC-dependent protein degradation is required to initiate bacterial adaptation mechanisms. We identified more than 100 putative ClpC target proteins through their stabilization in a clpC deletion strain. Beyond the identification of direct targets, we also observed indirect effects of the clpC deletion on the protein abundance in diverse cellular and metabolic pathways, such as iron acquisition and flagellar assembly. Overall, our data highlight the crucial role of ClpC for L. monocytogenes adaptation to the host environment through proteome remodeling. IMPORTANCE Survival and proliferation of pathogenic bacteria inside the host depend on their ability to adapt to the changing environment. Profiling the underlying changes on the bacterial proteome level during the infection process is important to gain a better understanding of the pathogenesis and the host-dependent adaptation processes. The cellular protein abundance is governed by the interplay between protein synthesis and decay. The direct readout of these events during infection can be accomplished using pulsed stable-isotope labeling by amino acids in cell culture (SILAC). Combining this approach with tandem-mass-tag (TMT) labeling enabled multiplexed and time-resolved bacterial proteome quantification during infection. Here, we applied this integrated approach to investigate protein turnover during the temporal progression of adaptation of the human pathogen L. monocytogenes to its host on a system-wide scale. Our experimental approach can easily be transferred to probe the proteome remodeling in other bacteria under a variety of perturbations.
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فهرسة مساهمة: Keywords: AAA+; ClpC; Listeria monocytogenes; adaptation; host-pathogen interactions; infection; mass spectrometry; proteolysis; proteomics; pulsed SILAC; tandem-mass-tag
تواريخ الأحداث: Date Created: 20210803 Latest Revision: 20240403
رمز التحديث: 20240403
مُعرف محوري في PubMed: PMC8407217
DOI: 10.1128/mSystems.00215-21
PMID: 34342529
قاعدة البيانات: MEDLINE
الوصف
تدمد:2379-5077
DOI:10.1128/mSystems.00215-21