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TitleStructural Basis of Pore Formation in the Mannose Phosphotransferase System by Pediocin PA-1.
Journal, issue, pagesAppl Environ Microbiol, Vol. 88, Issue 3, Page e0199221, Year 2022
Publish dateFeb 8, 2022
AuthorsLiyan Zhu / Jianwei Zeng / Chang Wang / Jiawei Wang /
PubMed AbstractBacteriocins are ribosomally synthesized bacterial antimicrobial peptides that have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like (or ...Bacteriocins are ribosomally synthesized bacterial antimicrobial peptides that have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like (or class IIa) bacteriocins (PLBs) exhibit antibacterial activity against several Gram-positive bacterial strains by forming pores in the cytoplasmic membrane of target cells with a specific receptor, the mannose phosphotransferase system (man-PTS). In this study, we report the cryo-electron microscopy structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1, the first and most extensively studied representative PLB, at resolutions of 3.12 and 2.45 Å, respectively. The structures revealed that the binding of pediocin PA-1 opens the Core domain of man-PTS away from its Vmotif domain, creating a pore through the cytoplasmic membranes of target cells. During this process, the N-terminal β-sheet region of pediocin PA-1 can specifically attach to the extracellular surface of the man-PTS Core domain, whereas the C-terminal half penetrates the membrane and cracks the man-PTS like a wedge. Thus, our findings shed light on a design of novel PLBs that can kill the target pathogenic bacteria. Listeria monocytogenes is a ubiquitous microorganism responsible for listeriosis, a rare but severe disease in humans, who become infected by ingesting contaminated food products (i.e., dairy, meat, fish, and vegetables): the disease has a fatality rate of 33%. Pediocin PA-1 is an important commercial additive used in food production to inhibit species. The mannose phosphotransferase system (man-PTS) is responsible for the sensitivity of Listeria monocytogenes to pediocin PA-1. In this study, we report the cryo-EM structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1 at resolutions of 3.12 and 2.45 Å, respectively. Our results facilitate the understanding of the mode of action of class IIa bacteriocins as an alternative to antibiotics.
External linksAppl Environ Microbiol / PubMed:34851716 / PubMed Central
MethodsEM (single particle)
Resolution2.45 - 3.12 Å
Structure data

32030

7vlx

EMDB-32030, PDB-7vlx:
Cryo-EM structures of Listeria monocytogenes man-PTS
Method: EM (single particle) / Resolution: 3.12 Å

32031

7vly

EMDB-32031, PDB-7vly:
Cryo-EM structure of Listeria monocytogenes man-PTS complexed with pediocin PA-1
Method: EM (single particle) / Resolution: 2.45 Å

Chemicals

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-HOH:
WATER

Source
  • listeria monocytogenes (bacteria)
  • pediococcus acidilactici (bacteria)
KeywordsMEMBRANE PROTEIN / antimicrobial peptides; bacteriocins; pediocin PA-1; pediocin-like/class IIa bacteriocins; antibiotic resistance; mannose phosphotransferase; man-PTS

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