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Updated: Jan 25, 2026

Comprehensive Autopsy Program for Individuals with Multiple Sclerosis
Published on: July 19, 2019
Structural analysis of a replication protein encoded by a plasmid isolated from a multiple sclerosis patient
Turgay Kilic1, Alexander N Popov2, Amelie Burk-Körner3
1Schaller Research Group at the University of Heidelberg, Heidelberg, Germany.
Abstract:
Bovine meat and milk factors (BMMFs) are circular, single-stranded episomal DNAs that have been detected in bovine meat and milk products. BMMFs are thought to have roles in human malignant and degenerative diseases. BMMFs encode a replication initiator protein (Rep) that is actively transcribed and translated in human cells. In this study, a Rep WH1 domain encoded on a BMMF (MSBI1.176) isolated from a multiple sclerosis human brain sample was determined to 1.53 Å resolution using X-ray crystallography. The overall structure of the MSBI1.176 WH1 domain was remarkably similar to other Rep structures, despite having a low (28%) amino-acid sequence identity. The MSBI1.176 WH1 domain contained elements common to other Reps, including five α-helices, five β-strands and a hydrophobic pocket. These new findings suggest that the MSBI1.176 Rep might have comparable roles and functions to other known Reps of different origins.
Insights
Bovine meat and milk factors (BMMFs) are circular DNA found in food. Researchers determined the structure of a BMMF Rep WH1 domain from a human brain, revealing similarities to other Reps.
Area of Science:
- Molecular Biology
- Structural Biology
- Virology
Background:
- Bovine meat and milk factors (BMMFs) are circular, single-stranded episomal DNAs found in bovine products.
- BMMFs are implicated in human malignant and degenerative diseases.
- BMMFs encode a replication initiator protein (Rep) that is transcribed and translated in human cells.
Purpose of the Study:
- To determine the high-resolution structure of a specific BMMF Rep WH1 domain (MSBI1.176) from a human multiple sclerosis brain sample.
- To compare the structure of MSBI1.176 Rep WH1 domain with other known Rep structures.
Main Methods:
- X-ray crystallography was used to determine the 3D structure of the MSBI1.176 Rep WH1 domain.
- The structure was resolved to a resolution of 1.53 Å.
Main Results:
- The MSBI1.176 Rep WH1 domain structure was determined at 1.53 Å resolution.
- Despite only 28% amino acid sequence identity, the MSBI1.176 Rep WH1 domain structure was highly similar to other Rep structures.
- Key structural features, including five α-helices, five β-strands, and a hydrophobic pocket, were conserved.
Conclusions:
- The MSBI1.176 Rep WH1 domain shares significant structural homology with other Rep proteins.
- These findings suggest that the MSBI1.176 Rep may possess similar functions and roles to other Reps from different origins.
- This structural information could be crucial for understanding BMMF roles in human diseases.
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