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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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AbstractAbstract 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.

Article
Mycobacterium tuberculosis PE_PGRS45 (Rv2615c) Promotes Recombinant Mycobacteria Intracellular Survival via Regulation of Innate Immunity, and Inhibition of Cell Apoptosis
Tao Xu , Chutong Wang , Minying Li , Jing Wei , Zixuan He , Zhongqing Qian , Xiaojing Wang , Hongtao Wang
J. Microbiol. 2024;62(1):49-62.   Published online February 9, 2024
DOI: https://doi.org/10.1007/s12275-023-00101-0
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  • 4 Web of Science
  • 4 Crossref
AbstractAbstract PDF
Tuberculosis (TB), a bacterial infectious disease caused by Mycobacterium tuberculosis (M. tuberculosis), is a significant global public health problem. Mycobacterium tuberculosis expresses a unique family of PE_PGRS proteins that have been implicated in pathogenesis. Despite numerous studies, the functions of most PE_PGRS proteins in the pathogenesis of mycobacterium infections remain unclear. PE_PGRS45 (Rv2615c) is only found in pathogenic mycobacteria. In this study, we successfully constructed a recombinant Mycobacterium smegmatis (M. smegmatis) strain which heterologously expresses the PE_PGRS45 protein. We found that overexpression of this cell wall-associated protein enhanced bacterial viability under stress in vitro and cell survival in macrophages. MS_PE_PGRS45 decreased the secretion of pro-inflammatory cytokines such as IL-1β, IL-6, IL-12p40, and TNF-α. We also found that MS_PE_PGRS45 increased the expression of the anti-inflammatory cytokine IL-10 and altered macrophage-mediated immune responses. Furthermore, PE_PGRS45 enhanced the survival rate of M. smegmatis in macrophages by inhibiting cell apoptosis. Collectively, our findings show that PE_PGRS45 is a virulent factor actively involved in the interaction with the host macrophage.

Citations

Citations to this article as recorded by  
  • Evolution of the PE_PGRS Proteins of Mycobacteria: Are All Equal or Are Some More Equal than Others?
    Bei Chen, Belmin Bajramović, Bastienne Vriesendorp, Herman Pieter Spaink
    Biology.2025; 14(3): 247.     CrossRef
  • Recent advances in research on Mycobacterium tuberculosis virulence factors and their role in pathogenesis
    Ming-Rui Sun, Jia-Yin Xing, Xiao-Tian Li, Ren Fang, Yang Zhang, Zhao-Li Li, Ning-Ning Song
    Journal of Microbiology, Immunology and Infection.2025; 58(5): 497.     CrossRef
  • Rv2741 Promotes Mycobacterium Survival by Modulating Macrophage Function via the IL-1α-MAPK Axis
    Xintong He, Yonglin He, Xichuan Deng, Nan Lu, Anlong Li, Sijia Gao, Shiyan He, Yuran Wang, Nanzhe Fu, Zijie Wang, Yuxin Nie, Lei Xu
    ACS Infectious Diseases.2025; 11(3): 676.     CrossRef
  • The PE/PPE family proteins of Mycobacterium tuberculosis: evolution, function, and prospects for tuberculosis control
    Zhijing Zhang, Le Dong, Xin Li, Taibing Deng, Qinglan Wang
    Frontiers in Immunology.2025;[Epub]     CrossRef

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