Grupo de Marcadores Inmunológicos, Laboratorio de Genética e Inmunología Molecular, Instituto de Biología, Pontificia Universidad Católica de Valparaíso, Valparaíso, Chile; Doctorado en Acuicultura, Programa Cooperativo Universidad de Chile Universidad, Universidad Católica del Norte, Pontificia Universidad Católica de Valparaíso, Chile.
Laboratorio de Fisiología y Genética Marina (FIGEMA), Departamento de Acuicultura, Facultad de Ciencias del Mar, Universidad Católica del Norte, Larrondo 1281, Coquimbo, Chile; Centro de Estudios Avanzados en Zonas Áridas (CEAZA), Larrondo 1281, Coquimbo, Chile.
Fish Shellfish Immunol. 2020 Feb;97:12-17. doi: 10.1016/j.fsi.2019.12.032. Epub 2019 Dec 13.
Lipopolysaccharide-binding proteins (LBPs) and bactericidal permeability-increasing proteins (BPIs) are effectors of the innate immune response which act in a coordinated manner to bind and neutralize the LPS present in Gram negative bacteria. The structural organization that confers the function of LBPs and BPIs is very similar, however, they are antagonistic to each other. In this work, we characterized two LBP/BPIs from the scallop Argopecten purpuratus, namely ApLBP/BPI1 and ApLBP/BPI2. The molecular and phylogenetic analyses of ApLBP/BPIs indicated that both isoforms display classic characteristics of LBP/BPIs from other invertebrates. Additionally, ApLBP/BPIs are constitutively expressed in scallop tissues and their transcript expression is upregulated in hemocytes and gills in response to an immune challenge. However, some structural characteristics of functional importance for the biological activity of these molecules, such as the net charge differ substantially between ApLBP/BPI1 and ApLBP/BPI2. Furthermore, each isoform displays a specific profile of basal expression among different tissues, as well as specific patterns of expression during the activation of the immune response. Results suggest that functional specialization of ApLBP/BPIs might happen, with potential role as LBP or BPI in this species of scallop. Further research on the biological activities of ApLBP/BPIs are necessary to elucidate their participation in the scallop immune response.
脂多糖结合蛋白（LBPs）和杀菌/通透性增加蛋白（BPIs）是先天免疫反应的效应物，它们以协调的方式结合并中和革兰氏阴性菌中存在的 LPS。赋予 LBPs 和 BPIs 功能的结构组织非常相似，但它们彼此拮抗。在这项工作中，我们从扇贝 Argopecten purpuratus 中鉴定了两种 LBP/BPI，即 ApLBP/BPI1 和 ApLBP/BPI2。ApLBP/BPI 的分子和系统发育分析表明，这两种同工型都显示了来自其他无脊椎动物的 LBP/BPI 的典型特征。此外，ApLBP/BPIs 在扇贝组织中持续表达，其转录表达在血细胞和鳃中被免疫挑战上调。然而，对于这些分子的生物学活性具有重要功能的一些结构特征，例如净电荷，在 ApLBP/BPI1 和 ApLBP/BPI2 之间有很大差异。此外，每种同工型在不同组织中的基础表达都有特定的模式，在免疫反应的激活过程中也有特定的表达模式。结果表明，ApLBP/BPIs 的功能特化可能发生，在这种扇贝中可能作为 LBP 或 BPI 发挥作用。进一步研究 ApLBP/BPIs 的生物学活性对于阐明它们在扇贝免疫反应中的参与是必要的。
