Human CXCR5 Virus-Like Particles

CXCR5, also known as C-X-C chemokine receptor type 5, is a G protein-coupled receptor (GPCR) that plays a key role in immune system regulation, particularly in the trafficking and homing of B cells and certain T cell subsets. This receptor specifically binds the chemokine CXCL13 (B lymphocyte chemoattractant, BLC), which is primarily secreted in lymphoid tissues such as lymph nodes, spleen, and Peyer''s patches. The CXCR5-CXCL13 axis is crucial for the organization of lymphoid follicles and the formation of germinal centers, where B cells undergo affinity maturation and differentiate into memory B cells or antibody-secreting plasma cells. CXCR5 is highly expressed on follicular helper T cells (Tfh), which are crucial for providing B cells with the signals required for antibody production. Dysregulation of CXCR5 signaling has been implicated in a variety of autoimmune diseases, lymphomas, and immunodeficiency, making it an important target for therapeutic research.

Human CXCR5 virus-like particles (VLPs) are non-infectious, self-assembling nanostructures that mimic the native conformation of CXCR5 on the cell surface. VLPs are typically produced by expressing CXCR5 and viral structural proteins (such as HIV Gag or hepatitis B core antigen) in eukaryotic systems to ensure proper post-translational modifications and membrane integration. These particles retain the structural and functional properties of CXCR5, including the ability to bind CXCL13, making them valuable tools for studying receptor-ligand interactions, antibody development, and vaccine design. Unlike soluble recombinant CXCR5, which may lack its native conformation, VLPs present the receptor in its native membrane-bound state, enhancing its immunogenicity and utility in immunological assays. CXCR5 VLPs are particularly suitable for generating monoclonal antibodies, screening for potential inhibitors, or developing vaccines against CXCR5-associated diseases, such as B-cell malignancies or autoimmune disorders.