MTB-LysB1: A Novel Endolysin Against Multidrug-resistant Mycobacterium tuberculosis

13 Jul 20264 min read0 viewsVerified Feed

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The phenotypic plasticity, slow replication, and complex, hydrophobic cell envelope of Mycobacterium tuberculosis contribute to its successful survival as a pathogen and its drug tolerance. Consequently, the global threat of multidrug-resistant Tuberculosis (MDR-TB), coupled with lengthy and highly toxic treatment regimens, necessitates the development of innovative treatment solutions.
Mycobacteriophages are natural viruses of mycobacteria that typically encode two endolysins, which cooperatively facilitate host cell lysis at the end of the lytic life cycle: LysA, a peptidoglycan hydrolase, and LysB, a lipolytic enzyme, targeting the mycolylarabinogalactan-peptidoglycan complex. Their precise and efficient lytic activity, along with their low propensity to induce resistance, make them, particularly LysBs, promising candidates for new treatment solutions.
In this study, we report MTB-LysB1, a novel LysB enzyme from an F1 sub-cluster mycobacteriophage isolated from our laboratory collection. While studying its structural features by comparing the modelled structure with representative mycobacteriophage LysB homologues, we found that the alpha/beta hydrolase fold and key motifs are conserved.
Also, we identified putative membrane-interaction motifs that may play a role in LysB1s cell permeation.

bioRxiv (Biomedical Preprints) published a clinical update in Research Highlights on 13 Jul 2026.

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bioRxiv (Biomedical Preprints)