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Published on: September 26, 2025
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Structural and biophysical characterization of Rv3716c, a hypothetical protein from Mycobacterium tuberculosis
A Gopalan1, G Deka2, M Prabhavathi1
1National Institute for Research in Tuberculosis, Chennai 600031, India.
Biochemical and Biophysical Research Communications
|November 21, 2017
Summary
Identifying new protein markers is crucial for diagnosing latent tuberculosis infection (LTBI). Researchers characterized MtbRv3716c, a potential LTBI marker, revealing its DNA-binding properties and structural features relevant for diagnosis.
Area of Science:
- Structural Biology
- Molecular Biology
- Biophysics
Background:
- Latent tuberculosis (LTBI) diagnosis remains a challenge for global TB elimination efforts.
- Current diagnostic tests for TB infection cannot differentiate between active disease and LTBI.
- Novel protein markers are needed for accurate LTBI diagnosis.
Purpose of the Study:
- To characterize the Mycobacterium tuberculosis protein Rv3716c (MtbRv3716c) as a potential diagnostic marker for LTBI.
- To elucidate the biophysical and structural properties of MtbRv3716c.
Main Methods:
- Electrophoretic Mobility Shift Assay (EMSA) to assess DNA binding.
- X-ray crystallography for structure determination at 1.9 Å resolution.
- Biophysical characterization of MtbRv3716c.
Main Results:
- MtbRv3716c was confirmed to bind double-stranded DNA.
- The crystal structure revealed a protomer that forms a dimer via crystal symmetry.
- The C-terminal region is proline-rich and intrinsically disordered, with potential roles in DNA binding.
- Cadmium ions mediate dimer packing, and large cavities suggest disordered termini.
Conclusions:
- MtbRv3716c exhibits DNA-binding capabilities, supporting its potential as a diagnostic marker for LTBI.
- Structural insights into MtbRv3716c provide a basis for understanding its function and potential applications.
- Further research into MtbRv3716c could lead to improved diagnostic tools for latent tuberculosis.
