A new linear polyketide, named aspormisin A (1), together with five known polyketides (2–6), were isolated from the alga-derived fungus Aspergillus ochraceopetaliformis SCSIO 41020. Their structures were elucidated through a detailed comprehensive spectroscopic analysis, as well as a comparison with the literature. An anti-inflammatory evaluation showed that compounds 2, 5, and 6 possessed inhibitory activity against the excessive production of nitric oxide (NO) and pro-inflammatory cytokines in LPS-treated RAW 264.7 macrophages in a dose-dependent manner without cytotoxicity. Further studies revealed that compound 2 was active in blocking the release of pro-inflammatory cytokines (IL-6, MCP-1, and TNF-α) induced by LPS both in vivo and in vitro. Our findings provide a basis for the further development of linear polyketides as promising anti-inflammatory agents.

Background: High-alcohol-producing Klebsiella pneumoniae (HiAlc Kpn ) can cause metabolic dysfunction-associated steatotic liver disease (MASLD) through sustained alcohol overflow in the microenvironment. As a probiotic, Bifidobacterium bifidum ( B. bifidum ) exhibits unique anti-inflammatory properties; however, whether and how it alleviate MASLD induced by HiAlc Kpn requires further investigation. Methods: MASLD mouse model was constructed by gavage administration with HiAlc Kpn W14 to assess the therapeutic effect of B. bifidum CIP-01 in vivo. Cell infection models, metabolomics sequencing, and in vitro antibacterial assays were integrated to systematically elucidate the mechanism by which B. bifidum CIP-01 mitigates HiAlc Kpn W14-induced cell damage. Results: B. bifidum CIP-01 was able to ameliorate MASLD induced by HiAlc Kpn through a multi-target mechanism. Compared to pair-fed mice, HiAlc Kpn W14 disrupted gut barrier and promoted inflammatory cytokines release. While, supplementation with B. bifidum CIP-01 reversed these effects by a) restoring intestinal integrity via upregulating tight junction proteins (ZO-1/Occludin) and mucin protein MUC-2, reducing reactive oxidative stress (ROS) and apoptosis in colonic cells, and b) rescuing hepatic cytochrome P450 2E1 (CYP2E1)-driven oxidative injury (ROS/Caspase-3) while promoting mitochondrial β -oxidation, as well as c) directly suppressing HiAlc Kpn proliferation and biofilm formation. Metabolomics and 16S rRNA of fecal samples analyses revealed B. bifidum CIP-01-mediated metabolic regulation: depletion of toxic branched-chain amino acids (BCAAs) intermediates and restoration of energy homeostasis and antioxidant defense alongside increased short-chain fatty acids (SCFAs)-associated pathways. Conclusion: Our findings highlight B. bifidum CIP-01 as a novel therapeutic candidate for HiAlc Kpn -induced MASLD, operating through a triad of pathogen suppression, gut–liver axis repair, and metabolic regulation.

Background/Objectives: The aim of this study was to clarify the antimicrobial susceptibility and distribution characteristics of Mycoplasma pneumoniae (M. pneumoniae, MP) collected from children in Beijing, China, from 2017 to 2025. Methods: A total of 197 MP isolates were analyzed. Mutations in macrolide-resistant loci of MP strains were detected via real-time fluorescent quantitative polymerase chain reactions. We used the broth microdilution method to determine the minimum inhibitory concentrations (MICs) of erythromycin, azithromycin, tetracycline, levofloxacin, and moxifloxacin against these isolates. The distribution characteristics of MIC values were further analyzed according to the isolates’ collection year, epidemic phase (low epidemic phase, epidemic initiation phase, ultra-low epidemic phase, outbreak phase, and epidemic recovery phase), and the corresponding patient age group (<3 years, 3–6 years, and ≥6 years). Results: All 197 isolates were found to be resistant to erythromycin and azithromycin, with a resistance rate of 100%. In contrast, the strains remained susceptible to tetracycline, levofloxacin and moxifloxacin. The highest resistance rate was 100% for macrolides. The MIC₉₀ values were 1024 μg/mL for erythromycin, 256 μg/mL for azithromycin, 0.5 μg/mL for tetracycline, 1 μg/mL for levofloxacin, and 0.125 μg/mL for moxifloxacin, respectively. Distinct differences in MIC distributions of erythromycin and azithromycin were observed across collection years, epidemic phases, and age groups. Conclusions: The resistance of MP to macrolides in children is closely associated with the epidemic intensity and age of the patient. Erythromycin is no longer suitable as an empirical therapy for MP infections during epidemic periods, whereas azithromycin can be cautiously administered in young children according to age stratification and MIC detection results. Meanwhile, it is imperative to strengthen the prevention and control of cluster MP infections during epidemic phases to reduce the transmission of drug-resistant MP strains.

This study aimed to use quantitative phosphoproteomics to explore phosphorylation characteristics in Klebsiella pneumoniae (Kpn)-induced liver abscess (KPLA) formation and liver injury. The Kpn strain LA-Kpn006 was phenotypically and genotypically characterized. A murine model of KPLA was established via intragastric inoculation. Phosphoproteomics and bioinformatic analyses were conducted to identify and quantify phosphosites and phosphoproteins. LA-Kpn006 displayed a hypermucoviscous phenotype, serotype K1, ST23 genotype, and harbored six major virulence genes. Inoculation induced liver colonization and typical histopathological abscess lesions. We quantified 3017 phosphoproteins covering 12,798 phosphosites (dominated by serine phosphorylation); 1723 proteins were upregulated and 425 downregulated. Bioinformatic analyses revealed remodeling in metabolism, stress response, signal transduction, and cytoskeleton organization. Upregulated proteins converged on fatty acid elongation, inositol phosphate metabolism, and the tricarboxylic acid cycle; downregulated proteins were enriched in PI3K–Akt, IL-17 signaling, and T-cell differentiation. Protein–protein interaction network analysis identified 10 key proteins (Src, Rac1, Actb, Hsp90aa1, Hsp90ab1, Egfr, Rps6, Pik3CA, Itgb1, and Fyn) that mediate inflammatory signaling, cytoskeleton remodeling, and immune infiltration. Dysregulated phosphorylation networks drive pathological metabolic adaptation, suppressed immune homeostasis, and cytoskeletal disorganization, collectively facilitating KPLA progression. The identified hub proteins and pathways represent high-value mechanistic targets and candidate therapeutic vulnerabilities for KPLA.