Related Experiment Video
Updated: Feb 6, 2026

Imaging Mycobacterium tuberculosis in Mice with Reporter Enzyme Fluorescence
Published on: February 26, 2018
Small Heat Shock Protein16.3 of Mycobacterium tuberculosis: After Two Decades of Functional Characterization
Babban Jee1, Yogesh Singh2, Renu Yadav3
1Department of Health Research, Ministry of Health and Family Welfare, Government of India, New Delhi, India.
Abstract:
Small heat shock proteins (sHSPs) are one of the five families of proteins acting as molecular chaperone. sHSPs possess a universally conserved alpha-crystallin domain, hence, also known as alpha-crystallin family. Mycobacterium tuberculosis (MTB) is an etiological agent of tuberculosis, a disease claiming million of lives every year across the world. MTB has two sHSPs: sHSP16.3 (a 16.3 kDa protein) and Acr2 (a 17.8 kDa protein). Of these, sHSP16.3 has been reported to be crucial for survival of MTB during prolonged period of dormancy, in addition to indispensable role in its growth, virulence and cell wall thickening. Additionally, this mycobacterial protein is also beneficial for host as well. Due to strong immunogenic properties and consistent presence in patients sera, sHSP16.3 has largely been implicated in vaccine development and diagnosis of latent and active infections of MTB in the clinical cases of TB. Recently, our study provided the substantial evidence to exploit this mycobacterial protein as a good drug target for developing novel therapeutic intervention. In the present review, a comprehensive analysis of various attributes of sHSP16.3 has been done and major gaps in area have been highlighted for future course of action.
Insights
Small heat shock proteins (sHSPs) are vital for Mycobacterium tuberculosis survival and virulence. Targeting sHSP16.3 offers a promising strategy for developing new tuberculosis therapeutics and diagnostics.
Area of Science:
- Molecular Biology
- Immunology
- Microbiology
Background:
- Small heat shock proteins (sHSPs) are molecular chaperones with a conserved alpha-crystallin domain.
- Mycobacterium tuberculosis (MTB), the cause of tuberculosis, possesses two sHSPs: sHSP16.3 and Acr2.
- sHSP16.3 is critical for MTB survival during dormancy, growth, virulence, and cell wall thickening.
Purpose of the Study:
- To comprehensively analyze the attributes of MTB's sHSP16.3.
- To highlight research gaps for future therapeutic and diagnostic development.
- To provide evidence for sHSP16.3 as a drug target.
Main Methods:
- Literature review and analysis of existing data on sHSP16.3.
- Examination of sHSP16.3's role in MTB physiology and host interaction.
- Assessment of sHSP16.3's immunogenic properties and diagnostic potential.
Main Results:
- sHSP16.3 plays a crucial role in MTB's survival, virulence, and dormancy.
- The protein is immunogenic and consistently detected in patient sera.
- sHSP16.3 presents a viable target for novel therapeutic interventions against TB.
Conclusions:
- sHSP16.3 is a key factor in MTB pathogenesis and survival.
- Its immunogenicity and essential role make it a promising candidate for TB vaccine development and diagnostics.
- Further research into sHSP16.3 is warranted for novel anti-TB strategies.
Related Concept Videos
Responses to Heat and Cold Stress
Shock Waves
When the source's speed approaches the speed of sound, constructive interference between successive wavefronts emitted by the source occurs immediately behind it. Initially, scientists believed that this constructive interference would result in such high...
Specific Heat
For example, increasing the temperature of one gram of water by 1°C requires one calorie of heat energy and can be written as 1 cal/g-°C, or...
Quantifying Heat
Heating and Cooling Curves
For instance, the addition of heat raises the temperature of a solid; the amount of heat absorbed depends on the heat capacity of the solid (q = mcsolidΔT). According to thermochemistry, the relation between the amount of heat absorbed or released by a substance, q, and its...
Heat Flow and Specific Heat

