Trichobilharzia regenti which are capable of keratin and collagen degradation. Experiments with laboratory prepared recombinant form of the cysteine peptidase cathepsin B2 of "T. regenti" (TrCB2) confirmed its ability to cleave skin proteins (collagen, keratin and elastin). After penetration the skin, cercariae transform to schistosomula and start a migration through the host’s body. They avoid penetration into blood capillaries and rather prefer entering peripheral nerves in host’s limbs. Schistosomula are found in peripheral nerves of ducks and mice as soon as 1.5 and 1 day post infection (DPI), respectively. In both types of hosts, schistosomula exhibit a high affinity to the central
Collagen receptor N-terminal domain rich in cystein, F2 fibronectin type II domain and several C-lectin domains. From this mannose family, collagen is specifically bound by mannose receptor, M-phospholipase A2 receptor and Endo180 receptor. Binding of collagen or denatured collagen (gelatin) is provided by F2 domain and partly by C-terminal domain (aa 1000-1453), which binds type I collagen triple helix. Inability to internalize collagen and reduced ability of adhesion and related increased migration in collagen matrix was observed in fibroblast population with nonfunctional Endo180 receptor. The exact principal of collagen binding to mannose receptor is not known so far. Endo180 receptor is expressed