4.3 Review

Diversity in heat shock protein families: functional implications in virus infection with a comprehensive insight of their role in the HIV-1 life cycle

期刊

CELL STRESS & CHAPERONES
卷 26, 期 5, 页码 743-768

出版社

SPRINGER
DOI: 10.1007/s12192-021-01223-3

关键词

HSP; Virus; Antiviral; HIV-1; HSP isoforms; Chaperones; HSP27; HSP40; HSP60; HSP70; HSP90; HSP110

资金

  1. Department of Biotechnology, Government of India COE project [BT/PR/15450/COE/34/46/2016]
  2. JC Bose Fellowship of SERB
  3. University Grants Commission
  4. Department of Biotechnology
  5. National Centre for Cell Science, Pune, India

向作者/读者索取更多资源

Heat shock proteins (HSPs) are cellular proteins induced during stress conditions, acting as chaperones that regulate protein folding and determine the fate of mis-folded/unfolded proteins. In viral infections, certain HSP isoforms play significant roles with varying pro-viral or anti-viral activities.
Heat shock proteins (HSPs) are a group of cellular proteins that are induced during stress conditions such as heat stress, cold shock, UV irradiation and even pathogenic insult. They are classified into families based on molecular size like HSP27, 40, 70 and 90 etc, and many of them act as cellular chaperones that regulate protein folding and determine the fate of mis-folded or unfolded proteins. Studies have also shown multiple other functions of these proteins such as in cell signalling, transcription and immune response. Deregulation of these proteins leads to devastating consequences, such as cancer, Alzheimer's disease and other life threatening diseases suggesting their potential importance in life processes. HSPs exist in multiple isoforms, and their biochemical and functional characterization still remains a subject of active investigation. In case of viral infections, several HSP isoforms have been documented to play important roles with few showing pro-viral activity whereas others seem to have an anti-viral role. Earlier studies have demonstrated that HSP40 plays a pro-viral role whereas HSP70 inhibits HIV-1 replication; however, clear isoform-specific functional roles remain to be established. A detailed functional characterization of all the HSP isoforms will uncover their role in cellular homeostasis and also may highlight some of them as potential targets for therapeutic strategies against various viral infections. In this review, we have tried to comprehend the details about cellular HSPs and their isoforms, their role in cellular physiology and their isoform-specific functions in case of virus infection with a specific focus on HIV-1 biology.

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