Back to Search
Start Over
Structure determination of CAMP factor of Mobiluncus curtisii and insights into structural dynamics.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2020 May 01; Vol. 150, pp. 1027-1036. Date of Electronic Publication: 2019 Nov 15. - Publication Year :
- 2020
-
Abstract
- Bacterial vaginosis (BV) is a common type of vaginal inflammation caused by a proliferation of pathogenic bacteria, among which Mobiluncus curtisii. In our previous studies on M. curtisii genome, we identified the presence of a genomic fragment encoding a 25 kDa pore-forming toxin, the CAMP factor, which is known to be involved in the synergistic lysis of erythrocytes namely CAMP reaction. However, whether this hypothetical gene product has hemolytic activity is unknown. Moreover, its relative structure and function are not yet solved. Here we found that the M. curtisii CAMP factor is a monomer at pH 4.4 and oligomer at pH > 4.6. Hemolysis assays showed that M. curtisii CAMP factor could lyse sheep red blood cells efficiently in pH 5.4-7.4. Negative staining electron microscope analysis of the CAMP factor revealed ring-like structures at pH above 4.6. Additionally, the crystal structure of M. curtisii CAMP factor, determineded at 1.85 Å resolution, reveals a 5 + 3 helix motif. Further functional analysis suggested that the structural rearrangement of the N-terminal domain might be required for protein function. In conclusion, this structure-function relationship study of CAMP factor provides a new perspective of the M. curtisii role in BV development.<br />Competing Interests: Declaration of Competing Interest The authors declare that they have no conflicts of interest with the contents of this article.<br /> (Copyright © 2019 Elsevier B.V. All rights reserved.)
- Subjects :
- Actinomycetales Infections genetics
Actinomycetales Infections metabolism
Animals
Bacterial Proteins genetics
Bacterial Proteins metabolism
Erythrocytes metabolism
Erythrocytes microbiology
Female
Humans
Mobiluncus genetics
Mobiluncus metabolism
Pore Forming Cytotoxic Proteins genetics
Pore Forming Cytotoxic Proteins metabolism
Protein Domains
Sheep
Structure-Activity Relationship
Vaginosis, Bacterial genetics
Vaginosis, Bacterial metabolism
Bacterial Proteins chemistry
Mobiluncus chemistry
Molecular Dynamics Simulation
Pore Forming Cytotoxic Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1879-0003
- Volume :
- 150
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 31739050
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2019.10.107