1. Recombinant protein production and functional analysis of a M60-like-2 metallopeptidase enzyme from the carcinogenic liver fluke Opisthorchis viverrini.
- Author
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Jumpajan J, Chaiyadet S, Saichua P, Tangkawatana S, Talabnin K, Laha T, and Suttiprapa S
- Subjects
- Cricetinae, Animals, Cattle, Carcinogens, Recombinant Proteins chemistry, Metalloproteases, Mucins, Opisthorchis genetics, Opisthorchis chemistry, Fasciola hepatica
- Abstract
Mucin plays a crucial role in safeguarding mucosal tissues by obstructing the translocation of microorganisms. Mucosal tissue-dwelling parasites must devise a strategy to surmount this mucin barrier in order to establish colonization. In a recent discovery, it was observed that the liver fluke Opisthorchis viverrini secretes two mucinases, namely Ov-M60-like-1 and Ov-M60-like-2. Ov-M60-like-1 was previously characterized. Here, we study the Ov-M60-like-2 by utilizing the wheat germ expression system to produce recombinant proteins and conducted a functional analysis of its enzymatic activity on bovine submaxillary mucin (BSM). Subsequently, we delved deeper into understanding the role of this enzyme in host-parasite interactions by evaluating its mucinase activity on mucins from the bile duct of O. viverrini-infected hamsters. Through successful production of recombinant proteins using the wheat germ expression system, we observed that this enzyme displayed mucinase activity over a wide pH range (pH 2 to pH 10) against BSM. Our investigations revealed it ability to digest mucin from the bile duct. These findings suggest that Ov-M60-like-2 possess a mucinase activity, together with Ov-M60-like-1, enabling the liver fluke to successful colonization of the host's bile duct., Competing Interests: Declaration of competing interest The authors declare there are no conflicts of interest., (Copyright © 2024. Published by Elsevier Inc.)
- Published
- 2024
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