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Leishmaniasis is a global health problem with an estimated report of 2 million new cases every year and more than 1 billion people at risk of contracting this disease in endemic areas. The innate immune system plays a central role in controlling  L .  major  infection by initiating a signaling cascade that results in production of pro-inflammatory cytokines and recruitment of both innate and adaptive immune cells. Upon infection with  L .  major , CXCL1 is produced locally and plays an important role in the recruitment of neutrophils to the site of infection. Herein, we report that  L .  major  specifically targets murine CXCL1 for degradation. The degradation of CXCL1 is not dependent on host factors as  L .  major  can directly degrade recombinant CXCL1 in a cell-free system. Using mass spectrometry, we discovered that the  L .  major  protease cleaves at the C-terminal end of murine CXCL1. Finally, our data suggest that  L .  major  metalloproteases are involved in the direct cleavage and degradation of CXCL1, and a synthetic peptide spanning the CXCL1 cleavage site can be used to inhibit  L .  major  metalloprotease activity. In conclusion, our study has identified an immune evasion strategy employed by  L .  major  to evade innate immune responses in mice, likely reservoirs in the endemic areas, and further highlights that targeting these  L .  major  metalloproteases may be important in controlling infection within the reservoir population and transmittance of the disease.

Leishmania major degrades murine CXCL1 – An immune evasion strategy