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Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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HSP-1-specific nanobodies alter chaperone function in vitro and in vivo
Nicholas D Urban1, Kunal Gharat2, Zachary J Mattiola1
1Department of Molecular & Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA.
The Journal of Biological Chemistry
|February 6, 2026
Summary
Researchers developed novel nanobodies, B12 and H5, to target heat shock protein 1 (HSP-1). These nanobodies inhibit HSP-1 activity, offering potential tools for aging and protein misfolding diseases.
Area of Science:
- Molecular Biology
- Cellular Biology
- Aging Research
Background:
- Heat shock proteins (HSP70) are crucial for cellular proteostasis.
- Dysfunctional protein folding and aggregation are linked to aging and diseases.
- Selective tools to modulate HSP70 chaperone activity are needed.
Purpose of the Study:
- To develop novel nanobodies targeting the HSP70 family member HSP-1.
- To investigate the inhibitory effects of these nanobodies on HSP-1 activity in vitro and in vivo.
- To assess the potential of these nanobodies as therapeutic tools for protein misfolding diseases and aging.
Main Methods:
- Development and characterization of two nanobodies (B12 and H5) against HSP-1.
- In vitro assays to measure HSP-1 ATPase activity and protein folding capacity inhibition.
- In vivo studies in transgenic Caenorhabditis elegans to assess stress resistance and survival.
Main Results:
- Nanobodies B12 and H5 specifically bind to recombinant and endogenous HSP-1.
- Both nanobodies dose-dependently inhibit HSP-1 ATPase activity and protein folding capacity in vitro.
- In vivo expression of nanobody B12 in C. elegans reduced stress resistance, mimicking hsp-1 knockdown.
Conclusions:
- Novel nanobodies B12 and H5 effectively inhibit HSP-1 chaperone activity.
- Nanobody B12 demonstrates in vivo efficacy in reducing stress resistance.
- These nanobodies represent promising tools for studying and potentially treating aging-related proteinopathies.
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