Molecular cloning and binding analysis of polymeric immunoglobulin receptor in largemouth bass (Micropterus salmoides). (May 2021)

• Record Type: Journal Article
• Authors: Yang, Shun; Yuan, Xiangyu; Kang, Ting; Xia, Yanting; Xu, Shuqi; Zhang, Xintang; Chen, Wenqi; Jin, Zhihong; Ma, Yuanxin; Ye, Zifeng; Qian, Shichao; Huang, Mengmeng; Lv, Zhengbing; Fei, Hui
• Is Part Of: Molecular immunology. Volume 133(2021)
• Page Start: 14
• Page End: 22
• Publication Date: 2021-05
• Subjects: Polymeric immunoglobulin receptor -- Micropterus salmoides -- Interaction -- IgM -- Bacteria; Immunochemistry -- Periodicals; Molecular biology -- Periodicals; Immunochemistry -- Periodicals; Allergy and Immunology -- Periodicals; Molecular Biology -- Periodicals; Immunochimie -- Périodiques; Biologie moléculaire -- Périodiques; Immunochemistry; Molecular biology; Periodicals; Electronic journals; 571.96
• DOI: 10.1016/j.molimm.2021.02.001
• Languages: English
• ISSNs: 0161-5890

Abstract

Graphical abstract: Highlights: Largemouth bass pIgR could combine with IgM. Largemouth bass pIgR could bind to Aeromonas hydrophila and Micrococcus luteus . Largemouth bass pIgR had binding capability to LPS, PGN and various saccharides. Saccharide binding was an important interaction mechanism between largemouth bass pIgR and bacteria. Abstract: The polymeric immunoglobulin receptor (pIgR) is an important molecule in the mucosal immunity of teleosts. Previous studies have shown that pIgR can bind and transport polymeric immunoglobulins (pIgs), but few studies have focused on the binding of teleost pIgR to bacteria. In this study, we identified a gene encoding pIgR in largemouth bass ( Micropterus salmoides ). The pIgR gene contained two Ig-like domains (ILDs), which were homologous to ILD1 and ILD5 of mammalian pIgR. Our results showed that largemouth bass pIgR-ILD could combine with IgM. Moreover, we also found that largemouth bass pIgR-ILD could bind to Aeromonas hydrophila and Micrococcus luteus . Further analysis showed that largemouth bass pIgR-ILD could also combine with lipopolysaccharide (LPS), peptidoglycan (PGN) and various saccharides, and reduced binding to bacteria was observed with LPS and PGN treatment, indicating that largemouth bass pIgR could bind to bacteria to prevent infection and that saccharide binding is an important interaction mechanism between pIgR and bacteria. These results collectively demonstrated that largemouth bass pIgR not only combines with IgM but also binds to bacteria by various saccharides.