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. 2017 Dec 5;8:1954. doi: 10.1038/s41467-017-02191-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Schematic of albumin/AlbiVax nanocomplexes for efficient vaccine delivery and combination cancer immunotherapy. a Upper: structure of HSA (PDB ID: 2BXH) and chemical structure of MEB; lower: schematic structure of albumin/MEB nanocomplexes (left) and 3D molecular structure predicted by molecular docking (right). Sticks represent MEB and the amino acid residues in the binding site I of HSA. Green dashed lines represent hydrogen bonds between MEB and amino acids. b Working mechanism of albumin/AlbiVax nanocomplexes as potent T cell vaccines. Left box: modular structures of AlbiCpG and albumin-binding Ag (AlbiAg). AlbiCpG were engineered by site specifically conjugating MEB and thiol-modified CpG, with hexaethyloxy-glycol (HEG) as tunable linkers; AlbiAg was synthesized by conjugating MEB and cysteine-modified Ags, including TAA and tumor-specific neoantigen discovered via exome sequencing. Left lower: locally administered AlbiVax binds to endogenous albumin and assembles into albumin/AlbiVax nanocomplexes, which were efficiently delivered to LNs due to lymphatic drainage and prolonged retention in LNs. Right: harnessing the endocytosis pathway of albumin, albumin/AlbiCpG and albumin/AlbiAg nanocomplexes were co-delivered into APCs and activated APCs for antigen cross presentation and clonal expansion of antigen-specific CD8⁺ CTLs, thereby eliciting robust and durable antitumor immunity. While albumin/AlbiVax nanocomplexes upregulated the expression of PD-1 on these CD8⁺ CTLs, combination of albumin/AlbiVax nanocomplexes with anti-PD-1 dramatically enhanced immunotherapeutic efficacy in established primary and metastatic tumors. The pharmacological behaviors of albumin/AlbiVax nanocomplexes were studied by quantitative PET imaging, light sheet fluorescence microscopy in whole cleared tissue, and super-resolution imaging in single APCs