Distinct vitellogenin domains differentially regulate immunological outcomes in invertebrates
| Autor: | Yue-Hong Zhao, Longwei Bai, Hao Li, Qun Wang, Yukai Qin, Weikang Sun, Wei-Wei Li |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
EspIgR E. sinensis polymeric immunoglobulin receptor Hemocytes Von Willebrand factor type D domain invertebrate immunology Biochemistry Bacterial Adhesion Vitellogenins Crustacea Phylogeny NJ neighbor-joining polymeric immunoglobulin receptor (pIgR) Cell biology LB Luria–Bertani Research Article hemocyte Protein domain pIg polyimmunoglobulin Biology 03 medical and health sciences Vitellogenin ORF open reading frame Phagocytosis Protein Domains pIgR polymeric immunoglobulin receptor vitellogenin (Vg) Animals Humans CPZ chlorpromazine Amino Acid Sequence Molecular Biology Vg vitellogenin Innate immune system 030102 biochemistry & molecular biology Bacteria Base Sequence HEK 293 cells VWD von Willebrand factor type D domain bacterial infection Cell Biology TBS Tris-buffered saline Open reading frame 030104 developmental biology HEK293 Cells biology.protein LLTP large lipid transfer protein SC secretory component Polymeric immunoglobulin receptor IPTG isopropyl b-D-1-thiogalactopyranoside Function (biology) |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 1083-351X 0021-9258 |
| Popis: | The classical role of Vitellogenin (Vg) is providing energy reserves for developing embryos, but its roles appear to extend beyond this nutritional function, and its importance in host immune defense is garnering increasing research attention. However, Vg-regulated immunological functions are dependent on three different domains within different species and remain poorly understood. In the present study, we confirmed three conserved VG domains—LPD_N, DUF1943, and VWD—in the Chinese mitten crab (Eriocheir sinensis), highlighting functional similarities of Vg in vertebrates and invertebrates. Of these three domains, DUF1943 and VWD showed definitive bacterial binding activity via interaction with the signature components on microbial surfaces, but this activity was not exhibited by the LPD_N domain. Antibacterial assays indicated that only the VWD domain inhibits bacterial proliferation, and this function may be conserved between different species due to the conserved amino acid residues. To further explore the relationship between Vg and polymeric immunoglobulin receptor (pIgR), we expressed EspIgR and the three E. sinensis Vg (EsVg) domains in HEK293T cells, and coimmunoprecipitation assay demonstrated that only the DUF1943 domain interacts with EspIgR. Subsequent experiments demonstrated that EsVg regulates hemocyte phagocytosis by binding with EspIgR through the DUF1943 domain, thus promoting bacterial clearance and protecting the host from bacterial infection. To the best of our knowledge, our work is the first to report distinct domains in Vg inducing different immunological outcomes in invertebrates, providing new evidence that pIgR acts as a phagocytic receptor for Vg. |
| Databáze: | OpenAIRE |
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