The Role of Heat Shock Proteins in Diseases and Their Therapeutic Potential: Environmental Stress and Microorganisms

A special issue of Microorganisms (ISSN 2076-2607). This special issue belongs to the section "Molecular Microbiology and Immunology".

Deadline for manuscript submissions: 15 July 2024 | Viewed by 3490

Special Issue Editors


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Guest Editor
College of Animal Science and Technology, Northeast Agricultural University, Harbin, China
Interests: environmental pollutants; toxicology; molecular mechanism
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Co-Guest Editor
Digital Agriculture Key Discipline of Jilin Province, Jilin Agricultural Science and Technology University, Jilin, China
Interests: heat shock proteins; environmental pollutants; diseases; therapy; molecular mechanism; toxicology

Special Issue Information

Dear Colleagues,

We are happy to announce this Special Issue of Microorganisms on "The role of Heat Shock Proteins in Diseases and Their Therapeutic Potential: Environmental stress and Microorganisms”. Microorganisms (ISSN: 2076-2607, IF 4.926) is an international, peer-reviewed open access journal related to prokaryotic and eukaryotic microorganisms, viruses, as well as prions.

Heat shock proteins (HSPs), a family of highly conserved proteins that that bind and help fold nascent or denatured polypeptides, ubiquitously exist in organisms (from bacteria to mammals). HSPs, also known as stress proteins, can change in case of disease occurrence and in the presence of environmental stressors such as microorganisms. Recent reports indicated that microorganisms played important role in the mechanism of biological injury induced by environmental stress.

In this Special Issue, our aim is to provide an in-depth view of "The Role of Heat Shock Proteins in Diseases and Their Therapeutic Potential: Environmental Stress including Biological Stress and Abiotic Stress and Microorganisms”. We welcome high-quality original research and review articles focusing on (but not limited to) the following subtopics:

  • Microorganisms
  • Heat Shock Proteins
  • Environmental stress
  • Diseases  
  • Therapy
  • Molecular mechanism
  • Environmental stress

Prof. Dr. Xiaohua Teng
Prof. Dr. You Tang
Guest Editors

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Keywords

  • microorganisms
  • heat shock proteins
  • environmental stress
  • diseases
  • therapy
  • molecular mechanism
  • microorganisms

Published Papers (2 papers)

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Review

25 pages, 3772 KiB  
Review
Insights and Perspectives on the Role of Proteostasis and Heat Shock Proteins in Fungal Infections
by João Neves-da-Rocha, Maria J. Santos-Saboya, Marcos E. R. Lopes, Antonio Rossi and Nilce M. Martinez-Rossi
Microorganisms 2023, 11(8), 1878; https://doi.org/10.3390/microorganisms11081878 - 25 Jul 2023
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Abstract
Fungi are a diverse group of eukaryotic organisms that infect humans, animals, and plants. To successfully colonize their hosts, pathogenic fungi must continuously adapt to the host’s unique environment, e.g., changes in temperature, pH, and nutrient availability. Appropriate protein folding, assembly, and degradation [...] Read more.
Fungi are a diverse group of eukaryotic organisms that infect humans, animals, and plants. To successfully colonize their hosts, pathogenic fungi must continuously adapt to the host’s unique environment, e.g., changes in temperature, pH, and nutrient availability. Appropriate protein folding, assembly, and degradation are essential for maintaining cellular homeostasis and survival under stressful conditions. Therefore, the regulation of proteostasis is crucial for fungal pathogenesis. The heat shock response (HSR) is one of the most important cellular mechanisms for maintaining proteostasis. It is activated by various stresses and regulates the activity of heat shock proteins (HSPs). As molecular chaperones, HSPs participate in the proteostatic network to control cellular protein levels by affecting their conformation, location, and degradation. In recent years, a growing body of evidence has highlighted the crucial yet understudied role of stress response circuits in fungal infections. This review explores the role of protein homeostasis and HSPs in fungal pathogenicity, including their contributions to virulence and host–pathogen interactions, as well as the concerted effects between HSPs and the main proteostasis circuits in the cell. Furthermore, we discuss perspectives in the field and the potential for targeting the components of these circuits to develop novel antifungal therapies. Full article
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17 pages, 627 KiB  
Review
New Insights into the Role and Therapeutic Potential of Heat Shock Protein 70 in Bovine Viral Diarrhea Virus Infection
by Nannan Chen, Tongtong Bai, Shuang Wang, Huan Wang, Yue Wu, Yu Liu and Zhanbo Zhu
Microorganisms 2023, 11(6), 1473; https://doi.org/10.3390/microorganisms11061473 - 01 Jun 2023
Cited by 2 | Viewed by 1584
Abstract
Bovine viral diarrhea virus (BVDV), a positive-strand RNA virus of the genus Pestivirus in the Flaviviridae family, is the causative agent of bovine viral diarrhea–mucosal disease (BVD-MD). BVDV’s unique virion structure, genome, and replication mechanism in the Flaviviridae family render it a useful [...] Read more.
Bovine viral diarrhea virus (BVDV), a positive-strand RNA virus of the genus Pestivirus in the Flaviviridae family, is the causative agent of bovine viral diarrhea–mucosal disease (BVD-MD). BVDV’s unique virion structure, genome, and replication mechanism in the Flaviviridae family render it a useful alternative model for evaluating the effectiveness of antiviral drugs used against the hepatitis C virus (HCV). As one of the most abundant and typical heat shock proteins, HSP70 plays an important role in viral infection caused by the family Flaviviridae and is considered a logical target of viral regulation in the context of immune escape. However, the mechanism of HSP70 in BVDV infection and the latest insights have not been reported in sufficient detail. In this review, we focus on the role and mechanisms of HSP70 in BVDV-infected animals/cells to further explore the possibility of targeting this protein for antiviral therapy during viral infection. Full article
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