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Recombinant protein production and functional analysis of a M60-like-2 metallopeptidase enzyme from the carcinogenic liver fluke Opisthorchis viverrini.
- Source :
-
Protein Expression & Purification . Apr2024, Vol. 216, pN.PAG-N.PAG. 1p. - Publication Year :
- 2024
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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. [Display omitted] • The carcinogenic liver fluke Opisthorchis viverrini releases Ov -M60-like-2 metallopeptidases. • Ov -M60-like-2 displays mucinase activity over a wide pH range (pH 2 to pH 10) against mucin substrate. • Ov -M60-like-2 digest mucin from the bile duct, allows the liver fluke colonize the bile duct of the host. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10465928
- Volume :
- 216
- Database :
- Academic Search Index
- Journal :
- Protein Expression & Purification
- Publication Type :
- Academic Journal
- Accession number :
- 175112845
- Full Text :
- https://doi.org/10.1016/j.pep.2024.106429