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The Mycobacteriophage Ms6 LysB N-Terminus Displays Peptidoglycan Binding Affinity

Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisboa, Portugal
UCIBIO-Applied Molecular Biosciences Unit, Departamento de Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2819-516 Caparica, Portugal
Laboratory of Bacterial Cell Surfaces and Pathogenesis, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Dann Turner
Viruses 2021, 13(7), 1377;
Received: 7 June 2021 / Revised: 1 July 2021 / Accepted: 12 July 2021 / Published: 15 July 2021
(This article belongs to the Special Issue Advances in Bacteriophage Biology)
Double-stranded DNA bacteriophages end their lytic cycle by disrupting the host cell envelope, which allows the release of the virion progeny. Each phage must synthesize lysis proteins that target each cell barrier to phage release. In addition to holins, which permeabilize the cytoplasmic membrane, and endolysins, which disrupt the peptidoglycan (PG), mycobacteriophages synthesize a specific lysis protein, LysB, capable of detaching the outer membrane from the complex cell wall of mycobacteria. The family of LysB proteins is highly diverse, with many members presenting an extended N-terminus. The N-terminal region of mycobacteriophage Ms6 LysB shows structural similarity to the PG-binding domain (PGBD) of the φKZ endolysin. A fusion of this region with enhanced green fluorescent protein (Ms6LysBPGBD-EGFP) was shown to bind to Mycobacterium smegmatis, Mycobacterium vaccae, Mycobacterium bovis BGC and Mycobacterium tuberculosis H37Ra cells pretreated with SDS or Ms6 LysB. In pulldown assays, we demonstrate that Ms6 LysB and Ms6LysBPGBD-EGFP bind to purified peptidoglycan of M. smegmatis, Escherichia coli, Pseudomonas aeruginosa and Bacillus subtilis, demonstrating affinity to PG of the A1γ chemotype. An infection assay with an Ms6 mutant producing a truncated version of LysB lacking the first 90 amino acids resulted in an abrupt lysis. These results clearly demonstrate that the N-terminus of Ms6 LysB binds to the PG. View Full-Text
Keywords: mycobacteriophage Ms6; LysB; phage lysis; mycobacteria; peptidoglycan binding mycobacteriophage Ms6; LysB; phage lysis; mycobacteria; peptidoglycan binding
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MDPI and ACS Style

Gigante, A.M.; Olivença, F.; Catalão, M.J.; Leandro, P.; Moniz-Pereira, J.; Filipe, S.R.; Pimentel, M. The Mycobacteriophage Ms6 LysB N-Terminus Displays Peptidoglycan Binding Affinity. Viruses 2021, 13, 1377.

AMA Style

Gigante AM, Olivença F, Catalão MJ, Leandro P, Moniz-Pereira J, Filipe SR, Pimentel M. The Mycobacteriophage Ms6 LysB N-Terminus Displays Peptidoglycan Binding Affinity. Viruses. 2021; 13(7):1377.

Chicago/Turabian Style

Gigante, Adriano M., Francisco Olivença, Maria J. Catalão, Paula Leandro, José Moniz-Pereira, Sérgio R. Filipe, and Madalena Pimentel. 2021. "The Mycobacteriophage Ms6 LysB N-Terminus Displays Peptidoglycan Binding Affinity" Viruses 13, no. 7: 1377.

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