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. 2021 Feb 12;11:603270. doi: 10.3389/fimmu.2020.603270

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Copyright © 2021 Jia, Jiang, Wang, Wang, Liu, Lv, Song, Li, Wang and Song

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Recombinant protein of CgDM9CP-4 preparation and verification of the pattern recognition function. (A) SDS-PAGE analysis of purified rCgDM9CP-4 protein and western-blot using the polyclonal antibody against CgDM9CP-4 in oyster hemocytes sample. (B–D) PAMPs binding (B), bacteria agglutination (C) and bacteria binding (D) activity of rCgDM9CP-4. ELISA assay was performed to determine the binding dissociated constant of rCgDM9CP-4 (0–12 μM) with LPS, Mannose, PGN and Glucan. Data are shown as the mean ± S.D. (N = 3). The data were curve-fitted using a single-site binding model. Bacteria agglutination activity of rCgDM9CP-4 was visualized by immunostaining by using FITC-labeled rat anti-his taq antibody after incubation of rCgDM9CP-4 with various microorganisms. Binding of rCgDM9CP-4 to Gram-positive, Gram-negative bacteria and fungi was measured by Western blotting analysis.