Journal of Microbiology

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I53-50: Engineered icosahedral protein cage for modular vaccine nanoplatform: Ke Liang, Shuang Wu, Sihang Dong, Tao Xu, Hongtao Wang; Received November 25, 2025 Accepted February 4, 2026 Published online April 6, 2026; DOI: https://doi.org/10.71150/jm.2511020 [Epub ahead of print]

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Abstract PDF: I53-50 is a computationally designed, self-assembling protein nanoparticle (NP) that forms a stable icosahedral structure composed of 120 protein subunits coordinated through precise interfacial interactions. Through unique intelligent regulation, I53-50 exhibits sensitivity to environmental signals and display multimodal “nano-smart” properties. I53-50 has a variety of modifiable surface-active sites, which facilitates precise chemical modification, gene fusion, tag coupling, and other functionalizations, thereby promoting effective lymphatic uptake and optimizing the immune response. I53-50 NPs show great potential in vaccine development, drug delivery, and biomaterials, representing a model fusion of computational biology and nanomedicine and offering a versatile tool for precision medicine.

Research Support, Non-U.S. Gov't

Surface Display of the HPV L1 Capsid Protein by the Autotransporter Shigella IcsA: Dan Xu , Xiaofeng Yang , Depu Wang , Jun Yu , Yili Wang; J. Microbiol. 2014;52(1):77-82. Published online January 4, 2014; DOI: https://doi.org/10.1007/s12275-014-3235-9

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Autotransporters have become attractive tools for surface expression of foreign proteins in Gram-negative bacteria. In this study, the Shigella autotransporter IcsA, has been exploited to express the human papillomavirus (HPV) type 16 L1 capsid protein in Shigella sonnei and Escherichia coli. The L1 gene was fused in-frame to replace the coding sequence of the IcsA passenger domain that is responsible for actin-based motility. The resultant hybrid protein could be detected by an anti-L1 antibody on the surface of S. sonnei and E. coli. In E. coli, the protein was expressed on the entire surface of the bacterium. In contrast, the protein was detected mainly at one pole of the Shigella bacterium. However, the protein became evenly distributed on the surface of the Shigella bacterium when the icsP gene was removed. Our study demonstrated the possibility of exploiting autotransporters for surface expression of large, heterologous viral proteins, which may be a useful strategy for vaccine development.

Citations

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