A type VI secretion system delivers a cell wall amidase to target bacterial competitors.
Bacteria
/ metabolism
Bacterial Proteins
/ metabolism
Cell Wall
/ metabolism
Gram-Negative Bacteria
/ metabolism
Metalloproteases
/ metabolism
N-Acetylmuramoyl-L-alanine Amidase
/ metabolism
Peptidoglycan
/ metabolism
Periplasm
/ metabolism
Pseudomonas aeruginosa
/ metabolism
Type VI Secretion Systems
/ metabolism
Virulence Factors
/ metabolism
beta-Lactamases
/ metabolism
bacterial competition
cell wall degradation
peptidoglycan hydrolase
type 6 secretion system
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
31
01
2020
revised:
02
04
2020
accepted:
02
04
2020
pubmed:
13
4
2020
medline:
15
7
2021
entrez:
13
4
2020
Statut:
ppublish
Résumé
The human pathogen Pseudomonas aeruginosa harbors three paralogous zinc proteases annotated as AmpD, AmpDh2, and AmpDh3, which turn over the cell wall and cell wall-derived muropeptides. AmpD is cytoplasmic and plays a role in the recycling of cell wall muropeptides, with a link to antibiotic resistance. AmpDh2 is a periplasmic soluble enzyme with the former anchored to the inner leaflet of the outer membrane. We document, herein, that the type VI secretion system locus II (H2-T6SS) of P. aeruginosa delivers AmpDh3 (but not AmpD or AmpDh2) to the periplasm of a prey bacterium upon contact. AmpDh3 hydrolyzes the cell wall peptidoglycan of the prey bacterium, which leads to its killing, thereby providing a growth advantage for P. aeruginosa in bacterial competition. We also document that the periplasmic protein PA0808, heretofore of unknown function, affords self-protection from lysis by AmpDh3. Cognates of the AmpDh3-PA0808 pair are widely distributed across Gram-negative bacteria. Taken together, these findings underscore the importance of their function as an evolutionary advantage and that of the H2-T6SS as the means for the manifestation of the effect.
Identifiants
pubmed: 32279364
doi: 10.1111/mmi.14513
pmc: PMC8011994
mid: NIHMS1591027
doi:
Substances chimiques
Bacterial Proteins
0
Peptidoglycan
0
Type VI Secretion Systems
0
Virulence Factors
0
AmpDh2 protein, Pseudomonas aeruginosa
EC 3.4.-
Metalloproteases
EC 3.4.-
AmpD protein, Bacteria
EC 3.5.1.28
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
beta-Lactamases
EC 3.5.2.6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
308-321Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM061629
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131685
Pays : United States
Informations de copyright
© 2020 John Wiley & Sons Ltd.
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