Circadian clocks are known to modulate host immune responses to pathogen infections, yet their role in influencing pathogen pathogenesis remains unclear. Here, Lu et al. identified the circadian clock components in Fusarium oxysporum and found reduced fungal pathogenicity in the clock mutants. The pathogenesis of F. oxysporum in plants is controlled by its circadian clock, with infections causing severe disease symptoms at dawn. The circadian clock regulates fungal pathogenicity by controlling the response to zinc starvation and secondary metabolite production.

Crosstalk between cell death programs confers appropriate host anti-infection immune responses, but how pathogens co-opt host molecular switches of cell death pathways to reprogram cell death modalities for facilitating infection remains largely unexplored. New findings by Prof. LIU and colleagues demonstrate that mycobacterial effector mammalian cell entry 3C (Mce3C) inhibits host cathepsin B (CTSB), a lysosome-derived non-caspase protease, to suppress host apoptosis while promoting necroptosis, hence exacerbating host immunopathology and facilitating bacterial survival.

HBEs distribute far beyond the territory of bacteria. In addition to ADP-heptose, many heptose nucleotidyltransferase that have a signature STTR5 motif are capable of synthesizing CDP-heptose, and sometimes UDP-heptose. Both CDP- and UDP-heptoses are effective agonists that can trigger innate immune responses via the ALPK1-TIFA axis similar to ADP-heptose.

Persistent infection of Mycobacterium tuberculosis (Mtb) has been linked to functional exhaustion of host immune cells including NK cells, but checkpoint molecules regulating this process remain largely unexplored. New findings by Prof. LIU and colleagues demonstrate that LILRB1, which is upregulated and activated by HLA-G upon Mtb infection, drives NK cell exhaustion in tuberculosis patients through inhibiting MAPK signaling, suggesting that LILRB1–HLA-G axis serves as a promising immunotherapy target for TB.

Prof. George Fu Gao's lab utilized cryo-EM to determine the apo S structures and their hACE2-bound structures of newly emerged variants BA.2.86, JN.1, EG.5, EG.5.1, and HV.1. The electrostatic changes and an additional N-glycosylation in BA.2.86 influence its binding to mAbs, and the JN.1 RBD L455S mutation maintains optimal receptor binding and enhances immune evasion.

This study uncovers that the CV-A10 virus contributes to onychomadesis in hand-foot-and-mouth disease by inhibiting Wnt/β-catenin signaling through KRM1 receptor invasion. It highlights the activation of the Wnt pathway as a potential treatment and offers novel insights into virus-host cellular signaling interactions.