Author

Mengjun Cheng

Fudan UniversityORCID 0000-0002-3271-7589Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Dongyang XuiD· 2 shared Jingxian LiuiD· 2 shared Lei ZhangiD· 2 shared Lian‐Wen QiiD· 2 shared Lijie GuoiD· 2 shared Meiling LüiD· 2 shared Meirong CheniD· 2 shared Nannan WuiD· 2 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersMicrobiology

Dongyang XuORCID

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2 papers

Recent·Most cited

Avs2 drives non-canonical tetrameric assembly of trypsin-like domain for anti-phage defense

Lijie Guo, Pingping Huang, Wenhui Liu, Jingxian Liu, Dongyang Xu, Shengbin Yu, Zongqiang Wang, Lei Zhang, Zhaoxing Li, Xu Cao, Qian Yang, Mengjun Cheng, Nannan Wu, Meiling Lü, Lian‐Wen Qi, , Meirong Chen

The paper elucidates the molecular mechanism of the Avs2-trypsin-MBL system, revealing how phage terminase recognition triggers tetramerization and activation of the system for anti-phage defense.

bioRxiv · Aug 26, 2026 · PreprintMicrobiology

The anti-phage mechanism of a widespread trypsin-MBL module

Pingping Huang, Jingxian Liu, Lijie Guo, Dongyang Xu, Lingbo Shen Shen, Purui Yan, Tong Chen, Wenying Fei, Mengjun Cheng, Zhaoxing Li, Meiling Lü, Lei Zhang, Nannan Wu, Lian‐Wen Qi, Yibei Xiao, Meirong Chen

This study identifies a trypsin-MBL module as a bacterial immune effector that uses proteolytic activation to enable DNase activity against invading nucleic acids while preventing self-toxicity.

bioRxiv · Sep 3, 2025 · PreprintBiochemistry