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A rare Tennessee outbreak of Mycobacterium fortuitum revealed deep gaps in infection prevention at outpatient surgery centers—where oversight, staffing, and reporting often fall short.

Summary: A humanized lung-on-a-chip model reveals early immune responses to Mycobacterium fortuitum infection, offering new insights into non-tuberculous mycobacteria pathogenesis relevant for drug…

HOYO-MiX · Genshin Impact - The Stellar Moments, Vol. 5 (Character Theme Original Soundtrack) · Song · 2025

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Mycobacteriophage MP2445 exhibits siphovirus morphology and infects <i>Mycobacterium smegmatis</i>, <i>Mycobacterium bovis</i> BCG, and <i>Mycobacterium fortuitum</i>. Its genome is 50,711 bp in length, has a GC content of 63.34%, and contains 78 protein-coding sequences and one tRNA. MP2445 shares …

Summary: A humanized lung-on-a-chip model reveals early immune responses to Mycobacterium fortuitum infection, offering new insights into non-tuberculous mycobacteria pathogenesis relevant for drug di...

HOYO-MiX · Genshin Impact - The Stellar Moments, Vol. 5 (Character Theme Original Soundtrack) · Song · 2025

The virulence-associated isonitrile lipopeptide (INLP) biosynthetic gene cluster is conserved across Mycobacterium tuberculosis and many nontuberculous mycobacteria (NTM) pathogens, yet the corresponding mycobacterial metabolites have not been fully characterized, and their biological functions are still debated. Here, we report a precursor neutral loss chromatography based mass spectrometry strategy that enables the targeted discovery of INLPs from Mycobacterium fortuitum, a fast-growing NTM pathogen. By monitoring a characteristic neutral loss of 27.1 Da corresponding to hydrogen cyanide, we identified a family of INLPs directly from bacterial culture extracts. Structural elucidation of a representative compound using NMR and high-resolution MS revealed a distinctive terminal methylated carboxyl group, contrasting with previously reported INLPs bearing linear alcohol, acetal, or cyclic motifs. Bioinformatic analysis and in vitro enzymatic assays identified a methyltransferase encoded within the INLP BGC responsible for methyl ester formation. Furthermore, metal-binding assays demonstrated selective chelation of Cu(I) and Cu(II) by the isolated INLP, but no detectable interaction with Zn(II), suggesting a role in copper homeostasis. These findings represent the first full structural characterization of an INLP from pathogenic mycobacteria, expand our understanding of the enzymes involved in INLP modification, and unequivocally support the copper-binding activity of INLPs from these pathogens.