Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

• Published in: Experimental parasitology 2014-09, Vol.144, p.27-33
• Main Authors: Yu, Changmao, Wang, Yinan, Zhang, Jing, Fang, Wenzhen, Luo, Damin
• Format: Article
• Language: English
• Subjects: Angiostrongylus cantonensis; Angiostrongylus cantonensis - enzymology; Angiostrongylus cantonensis - genetics; Angiostrongylus cantonensis - growth & development; Animals; Blotting, Western; Cathepsin B - genetics; Cathepsin B - isolation & purification; Cathepsin B - metabolism; Cathepsin B cysteine protease; Cloning, Molecular; Developmental expression pattern; DNA, Complementary - genetics; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation, Developmental; Gene Expression Regulation, Enzymologic; Immunolocalization; Mice; Microscopy, Fluorescence; Rats; Rats, Sprague-Dawley; Real-Time Polymerase Chain Reaction; Snails
• ISSN: 0014-4894; 1090-2449
• DOI: 10.1016/j.exppara.2014.06.008

[Display omitted] •Evidences were provided for AC-cathB-1 and -2 to be the ES proteins in larvae.•Anatomic sites and expression patterns of the two AC-cathBs were varied.•Only AC-cathB-2 was detected in genital system, especially in wall of genital tracts.•AC-cathB-2 might be involved in germ cells development and maturation.•AC-cathB-1, -2 differ in substrate specificities and precise physiological functions. In this study we have investigated the anatomic sites of expression and developmental expression patterns of two cathepsin B-like cysteine proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis. The immunolocalization results revealed that native AC-cathBs were found present in the L1 and L3 larvae, female and male adults, and the AC-cathBs were localized mainly on the digestive tract of A. cantonensis and expressed at varied levels and in different patterns in the internal tissues according to their developmental stage. Consistent with the infective stage of L3 is a much more intense staining of AC-cathBs in the esophagus compared with the intestine. In contrast to L3, more abundant signals were located to the intestine of adults, suggesting that nutrition digestion likely to be the main function of the protease at this point. AC-cathBs fluorescent signals were present in excretory pore, excretory tube in lateral cords, and muscular esophagus of larvae, further supported the AC-cathB-1, -2 likely to be released by A. cantonensis as excretory/secretory products. Additionally, only the protein AC-cathB-2 was detected in the reproductive system, especially in the wall of vas deferens, uterus, and oviduct of the parasites, whether the AC-cathB-2 has some function in germ cells development and maturation need to be further characterized. Although the anatomic sites and expression patterns were different in larvae and adults and the corresponding function might not the same, AC-cathB-1 and -2 involved in the host-parasite interaction in addition to digestive function.