A viral protein antibiotic inhibits lipid II flippase activity.
Nat Microbiol
; 2(11): 1480-1484, 2017 Nov.
Article
en En
| MEDLINE
| ID: mdl-28894177
ABSTRACT
For bacteriophage infections, the cell walls of bacteria, consisting of a single highly polymeric molecule of peptidoglycan (PG), pose a major problem for the release of progeny virions. Phage lysis proteins that overcome this barrier can point the way to new antibacterial strategies 1 , especially small lytic single-stranded DNA (the microviruses) and RNA phages (the leviviruses) that effect host lysis using a single non-enzymatic protein 2 . Previously, the A2 protein of levivirus Qß and the E protein of the microvirus ÏX174 were shown to be 'protein antibiotics' that inhibit the MurA and MraY steps of the PG synthesis pathway 2-4 . Here, we investigated the mechanism of action of an unrelated lysis protein, LysM, of the Escherichia coli levivirus M 5 . We show that LysM inhibits the translocation of the final lipid-linked PG precursor called lipid II across the cytoplasmic membrane by interfering with the activity of MurJ. The finding that LysM inhibits a distinct step in the PG synthesis pathway from the A2 and E proteins indicates that small phages, particularly the single-stranded RNA (ssRNA) leviviruses, have a previously unappreciated capacity for evolving novel inhibitors of PG biogenesis despite their limited coding potential.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Uridina Difosfato Ácido N-Acetilmurámico
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Proteínas Virales
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Peptidoglicano
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Levivirus
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Proteínas de Escherichia coli
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Proteínas de Transferencia de Fosfolípidos
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Escherichia coli
Idioma:
En
Revista:
Nat Microbiol
Año:
2017
Tipo del documento:
Article
País de afiliación:
Estados Unidos