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ClpB通过独立于DnaK的蛋白质解聚作用增强热耐受性。

ClpB enhances thermotolerance in through protein disaggregation independent of DnaK.

作者信息

Hur Jeong In, Kim Jinshil, Ryu Sangryeol, Jeon Byeonghwa

机构信息

Department of Food and Animal Biotechnology, Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul, South Korea.

Department of Agricultural Biotechnology, Seoul National University, Gwanak-gu, Seoul, South Korea.

出版信息

Microbiol Spectr. 2025 Jun 3;13(6):e0229324. doi: 10.1128/spectrum.02293-24. Epub 2025 Apr 30.

DOI:10.1128/spectrum.02293-24
PMID:40304467
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12131804/
Abstract

is a leading cause of foodborne infections worldwide and primarily transmitted to humans through the consumption of contaminated poultry meat. To enhance -associated food safety, it is critical to understand how survives during the thermal processing of poultry products. In this study, we monitored the survival of 86 . strains during heat treatment and observed that some strains exhibited elevated heat tolerance. Notably, multilocus sequence typing clonal complex (CC)-443 and CC-607 were dominant among heat-tolerant strains, while the CC-21 strains were mostly heat-sensitive, indicating phylogenetic association with thermotolerance. We also investigated the function of heat shock chaperones in the thermotolerance of . Among several knockout mutants of heat shock chaperones, a mutant lacking exhibited significantly lower survival than the wild type under heat treatment. Moreover, we observed a significantly higher accumulation of protein aggregates in the absence of , demonstrating that ClpB functions as a disaggregase during heat exposure. Additionally, ClpB from the heat-tolerant CC-443 group possessed distinct amino acid substitutions in the functional nucleotide-binding domain compared to ClpB in other CC groups. Interestingly, despite the well-known interaction of these proteins in many other bacteria, a two-hybrid assay demonstrated that ClpB of does not bind to DnaK, suggesting that may have a distinct mechanism for protein disaggregation and stress tolerance. Our findings demonstrate that ClpB plays a crucial role in the thermotolerance of through unique protein disaggregation mechanisms during poultry processing.IMPORTANCEThis study unveils a distinctive mechanism of thermotolerance involving protein disaggregation in , a major foodborne pathogen. Understanding 's ability to withstand heat stress is crucial for comprehending the occurrence of infections resulting from the consumption of contaminated poultry meat. Our research elucidates the roles of heat shock proteins, particularly ClpB, in the thermotolerance of . These findings significantly contribute to our fundamental understanding of bacterial physiology related to stress tolerance, which has important implications for public health and food safety.

摘要

是全球食源性感染的主要原因,主要通过食用受污染的禽肉传播给人类。为提高与相关的食品安全,了解在禽产品热加工过程中的存活情况至关重要。在本研究中,我们监测了86株菌株在热处理过程中的存活情况,观察到一些菌株表现出较高的耐热性。值得注意的是,多位点序列分型克隆复合体(CC)-443和CC-607在耐热菌株中占主导地位,而CC-21菌株大多对热敏感,表明与耐热性存在系统发育关联。我们还研究了热休克伴侣蛋白在耐热性中的作用。在几种热休克伴侣蛋白的基因敲除突变体中,缺乏的突变体在热处理下的存活率明显低于野生型。此外,我们观察到在缺乏时蛋白质聚集体的积累显著增加,表明ClpB在热暴露期间作为解聚酶发挥作用。此外,与其他CC组中的ClpB相比,耐热CC-443组的ClpB在功能性核苷酸结合结构域中具有不同的氨基酸取代。有趣的是,尽管这些蛋白质在许多其他细菌中存在众所周知的相互作用,但双杂交试验表明的ClpB不与DnaK结合,这表明可能具有独特的蛋白质解聚和应激耐受机制。我们的研究结果表明,ClpB通过在禽肉加工过程中独特的蛋白质解聚机制在耐热性中起关键作用。重要性本研究揭示了一种主要食源性病原体中涉及蛋白质解聚的独特耐热机制。了解耐受热应激的能力对于理解食用受污染禽肉导致感染的发生至关重要。我们的研究阐明了热休克蛋白,特别是ClpB,在耐热性中的作用。这些发现极大地有助于我们对与应激耐受相关的细菌生理学的基本理解,这对公共卫生和食品安全具有重要意义。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/b4ea8a59590b/spectrum.02293-24.f005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/2f5ceddcfadc/spectrum.02293-24.f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/7472e8160271/spectrum.02293-24.f002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/b23fd9ed1558/spectrum.02293-24.f003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/18ddce1d2dc2/spectrum.02293-24.f004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/b4ea8a59590b/spectrum.02293-24.f005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/2f5ceddcfadc/spectrum.02293-24.f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/7472e8160271/spectrum.02293-24.f002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/b23fd9ed1558/spectrum.02293-24.f003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/18ddce1d2dc2/spectrum.02293-24.f004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2eca/12131804/b4ea8a59590b/spectrum.02293-24.f005.jpg

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Front Microbiol. 2024 Nov 22;15:1493849. doi: 10.3389/fmicb.2024.1493849. eCollection 2024.
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