AI Article Synopsis
- A novel protein called MaTWD, containing three whey acidic protein domains (WAPDs), was discovered in the weather loach (Misgurnus anguillicaudatus) and is linked to immune response.
- MaTWD exhibits a high similarity to WAPDs in fish, but a low similarity with those in other animal groups, suggesting a specialized function in fish.
- The study showed that MaTWD has the ability to bind bacteria, exhibit antimicrobial properties, and protect loaches from bacterial infections, highlighting its role in antibacterial immunity through antiprotease activity.
Article Abstract
Whey acidic protein domain (WAPD) occurs in a variety of proteins in animals and many of WAPD-containing proteins are involved in immunity. In the present study, a novel protein containing three WAPDs was identified from the weather loach, Misgurnus anguillicaudatus, designated as MaTWD. MaTWD share high identity with TWDs from fish but low identity with TWDs from other animal phyla. MaTWD transcripts mainly distributed in gills and head kidney responded to bacterial challenge with significant upregulation. In vitro assay with recombinant MaTWD protein revealed that MaTWD had antiprotease activity against bacterial proteases. Moreover, MaTWD exhibited bacterial binding capacity and antimicrobial activity. Most importantly, exogenous MaTWD protected loach against bacterial infection by reducing loach mortality. We infer that MaTWD participates in the antibacterial immunity of loach via its antiprotease and antimicrobial activities.
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| http://dx.doi.org/10.1016/j.fsi.2020.05.032 | DOI Listing |
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