Molecular Basis of Angicin Activity
Vogel, V.; Rodriguez, A.; Kruszewska-Naczk, B.; Mauerer, S.; Olari, L.-R.; Köhler, J.; Yadav, P.; Apolloni, J.; Read, C.; Walther, P.; Weidinger, G.; Münch, J.; Ständker, L.; Spellerberg, B.
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Angicin is a class IId bacteriocin produced by Streptococcus anginosus with activity against Gram-positive pathogens, including Listeria monocytogenes and vancomycin-resistant Enterococcus faecium. While the mannose phosphotransferase system (Man-PTS) has been identified as a receptor in L. monocytogenes, its role in streptococci and the structural determinants of Angicin activity remain unclear. Here, we demonstrate that the Man-PTS is required for Angicin susceptibility in Streptococcus constellatus. A transposon mutant (manM::ISS1) showed complete resistance to Angicin and impaired mannose utilization. Structure-activity relationship analysis of truncated and modified peptides localized antimicrobial activity to the C-terminal region, although none of the variants matched the activity of the full-length peptide. Angicin induced membrane depolarization and pore formation in target bacteria. Residual activity in Man-PTS-impaired L. monocytogenes suggests an additional receptor-independent effect at higher concentrations. In vivo toxicity analysis using zebrafish embryos showed low toxicity at active concentrations. These findings identify the Man-PTS as a receptor for Angicin in streptococci and define structural features associated with its antimicrobial activity.
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