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Metalloproteases (MPs) have demonstrated roles in immune modulation. In some cases, these enzymes are produced by parasites to influence host immune responses such that parasite infection is facilitated. One of the best examples of parasite-mediated immune modulation is the matrix metalloprotease (MMP) leishmanolysin (Gp63), which is produced by species of the genus  Leishmania  to evade killing by host macrophages. Leishmanolysin-like proteins appear to be quite common in many invertebrates, however our understanding of the functions of these non-leishmania enzymes is limited. Numerous proteomic and transcriptomic screens of schistosomes, at all life cycle stages of the parasite, have identified leishmanolysin-like MPs as being present in abundance; with the highest levels being found during the intramolluscan larval stages and being produced by cercaria. This study aims to functionally characterize a  Schistosoma mansoni  variant of leishmanolysin that most resembles the enzyme produced by  Leishmania , termed SmLeish. We demonstrate that SmLeish is an important component of  S .  mansoni  excretory/secretory (ES) products and is produced by the sporocyst during infection. The presence of SmLeish interferes with the migration of  Biomphalaria glabrata  haemocytes, and causes them to present a phenotype that is less capable of sporocyst encapsulation. Knockdown of SmLeish in  S .  mansoni  miracidia prior to exposure to susceptible  B .  glabrata  reduces miracidia penetration success, causes a delay in reaching patent infection, and lowers cercaria output from infected snails.

plos pathogens

A metalloprotease produced by larval Schistosoma mansoni facilitates infection establishment and maintenance in the snail host by interfering with immune cell function