Methods: In the present study, we successfully identified the open reading frame encoding the metalloproteinase of
Results: No VCAM-1 proteolysis was identified from exotoxins collected from mutant strain cultures. Additionally, a recombinant form of the Mcs1 protease retained functional VCAM-1 cleavage activity. Computational analytics confirmed the protein-protein interaction between Mcs1 and VCAM-1 bound molecules.
Conclusion: This study represents the identification and characterization of a novel metalloproteinase that directly modifies adhesions critical to the retention of hematopoietic precursors to the bone marrow environment. Better understanding the role of Mcs1 in the development of LR and the pathogenesis of C. sordelliiinfection may lead to the development of novel diagnostic tools or therapeutic strategies that could limit the morbidity and mortality associated with this deadly infection.
E. Mcindoo, None
J. French, None
D. Stevens, None