The Mycobacteriophage Ms6 LysB
| Autor: | José Moniz-Pereira, Adriano M Gigante, Paula Leandro, Francisco Olivença, Maria João Catalão, Madalena Pimentel, Sergio R. Filipe |
|---|---|
| Přispěvatelé: | DCV - Departamento de Ciências da Vida, UCIBIO - Applied Molecular Biosciences Unit, Instituto de Tecnologia Química e Biológica António Xavier (ITQB) |
| Rok vydání: | 2021 |
| Předmět: |
peptidoglycan binding
mycobacteria Lysin Peptidoglycan binding Bacillus subtilis Peptidoglycan Microbiology Article Mycobacterium 03 medical and health sciences chemistry.chemical_compound Viral Proteins phage lysis Bacteriolysis SDG 3 - Good Health and Well-being LysB Cell Wall Virology Endopeptidases 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry Mycobacterium smegmatis Hydrolysis Cell Membrane Mycobacteria Phage lysis Mycobacteriophages biology.organism_classification QR1-502 Infectious Diseases Biochemistry Lytic cycle Host cell envelope mycobacteriophage Ms6 Bacterial outer membrane Mycobacteriophage Ms6 Protein Binding |
| Zdroj: | Viruses, Vol 13, Iss 1377, p 1377 (2021) Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP Viruses Volume 13 Issue 7 |
| ISSN: | 1999-4915 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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