The function and structure determination of CAMP factor of M. curtisii is published.
Release time:2019-11-25 Browse:64

The function and structure determination of CAMP factor of M. curtisii is published.

Dr. Weihong Zeng’s manuscript titled with Structure determination of CAMP factor of Mobiluncus curtisii and insights into structural dynamics was published online at In J Biol Macromol on Nov 15th, 2019. Congratulations.

Currently, the co-first authors of this paper are Weihong Zeng at Jinan University and Huan Ma at USTC. Prof. Tengchuan Jin of USTC and Prof. Meixiang Yang at Jinan University are corresponding authors. Congratulations to all authors.


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.