Cathepsin L (CTSL) as a cysteine cathepsin protease mediates complement C3 cleavage and pathogen degradation. In the present study, a CTSL homolog was identified from Crassostrea gigas (designated as CgCTSL-2). Its mRNA expression increased significantly in hemocytes after Vibrio splendidus stimulation. The activity of rCgCTSL-2 was induced after incubation with LPS or V. splendidus in Ca2+-dependent manner. rCgCTSL-2 could specifically bound V. splendidus in Ca2+-dependent manner. The co-localization of rCgCTSL-2 and V. splendidus was observed in cell-free hemolymph. Upon binding V. splendidus, CgCTSL-2 interacted with CgC3 in cell-free hemolymph and hemocytes. CgC3 fragments in CgCTSL-2-RNAi oysters and full length CgC3 in rCgCTSL-2-treated oysters were both reduced in cell-free hemolymph, respectively. CgC3 fragments were accumulated in CgCTSL-2-RNAi or rCgCTSL-2-treated oysters. The co-localizations of V. splendidus, CgC3, CgCD18, CgCTSL-2 and lysosomes were observed in hemocytes. These results suggested that CgCTSL-2 upon binding V. splendidus directly interacted with CgC3 to lead to CgC3 cleavage and then CgC3 fragments coated on V. splendidus were mediated by CgCD18 into CTSL-2-lysosome pathway. [ABSTRACT FROM AUTHOR]

Copyright of Cell Communication & Signaling is the property of BioMed Central and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)