| 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. |
Publication
Journal Publication
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