Source: INDIATODAY
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The team from JNU's Special Centre for Molecular Medicine, identified a human protein, Hsp70, as a critical factor in the spread of diseases like malaria and Covid-19.
Working alongside Indian and Russian researchers the team has developed a small molecule inhibitor that could revolutionize treatments for multiple infectious diseases.
Read about Malaria: https://www.iasgyan.in/daily-current-affairs/malaria-2
Read about covid variants: https://www.iasgyan.in/daily-current-affairs/new-covid-variants
The researchers developed and tested PES-Cl a small molecule inhibitor of Hsp70.
The researchers successfully inhibited SARS-CoV-2 replication in infected cells at a low dose.
The researchers demonstrated potential to block the replication of malaria parasites.
The research highlighted the effectiveness of host-targeting antivirals which are less likely to face resistance compared to traditional antiviral drugs.
Aspect |
Benefit |
Reduced Drug Resistance |
Viruses cannot easily mutate host proteins to evade the drug's action. |
Broad-Spectrum Action |
Effective against multiple pathogens using similar host machinery. |
Preparedness |
Helps tackle rapidly evolving pathogens and variants like Omicron. |
Heat Shock Protein 70 (HSP70) is a molecular chaperone that plays a crucial role in protein folding, stabilization and cellular stress response. This highly conserved protein family is critical for maintaining cellular homeostasis especially under stress conditions like heat, toxins and infections.
Molecular chaperones are defined as proteins that assists in the folding, assembly and conformational maintenance other proteins without becoming part of its final structure.
Characteristic |
Description |
Molecular Weight |
Approximately 70 kDa. |
Conservation |
Highly conserved across species from bacteria to humans. |
Induction |
Expression increases under stress conditions such as heat shock. |
Localization |
Found in various cellular compartments, including cytosol, nucleus and organelles. |
Process |
Role of HSP70 |
Protein Quality Control |
Ensures the proper folding and degradation of damaged proteins. |
Stress Response |
Increases expression to protect cellular machinery during stress. |
Signal Transduction |
Modulates pathways by stabilizing signaling proteins. |
Cancer |
Overexpressed in tumors aiding in survival under hypoxic and acidic conditions. |
Neuroprotection |
Reduces protein aggregation in neurodegenerative diseases like Alzheimer's. |
Application |
Description |
Cancer Therapy |
Inhibitors of HSP70 being studied for tumor suppression. |
Neuroprotection |
Enhancing HSP70 expression to combat neurodegenerative diseases. |
Vaccine Development |
Acts as an adjuvant to enhance immune responses in vaccines. |
Cardioprotection |
Preconditioning therapies to protect cardiac tissues during ischemic events. |
Sources:
PRACTICE QUESTION Q.With reference to Heat Shock Protein 70 (HSP70), consider the following statements:
Which of the statements given above is/are correct? (a) 1 only (b) 2 and 3 only (c) 1 and 3 only (d) 1, 2 and 3 Answer: (b) Explanation: Statement 1 is incorrect. HSP70 is not exclusively found in the cytoplasm; it is present in various cellular compartments including the cytoplasm, nucleus, mitochondria and even extracellular spaces depending on the isoform. Statement 2 is correct. HSP70 plays a vital role as a molecular chaperone assisting in the folding of newly synthesized proteins and refolding misfolded proteins during stress conditions. Statement 3 is correct. The expression of HSP70 is upregulated in response to stress conditions like heat shock, oxidative stress and exposure to toxins making it a critical component of the cellular stress response. |
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