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Patatin-like phospholipase CapV in Escherichia coli - morphological and physiological effects of one amino acid substitution
In rod-shaped bacteria, morphological plasticity occurs in response to stress, which blocks cell division to promote filamentation. We demonstrate here that overexpression of the patatin-like phospholipase variant CapV Q329R , but not CapV, causes pronounced sulA -independent pyridoxine-inhibited ce...
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Published in: | NPJ biofilms and microbiomes 2022-05, Vol.8 (1), p.39-18, Article 39 |
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Main Authors: | , , , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | In rod-shaped bacteria, morphological plasticity occurs in response to stress, which blocks cell division to promote filamentation. We demonstrate here that overexpression of the patatin-like phospholipase variant CapV
Q329R
, but not CapV, causes pronounced
sulA
-independent pyridoxine-inhibited cell filamentation in the
Escherichia coli
K-12-derivative MG1655 associated with restriction of flagella production and swimming motility. Conserved amino acids in canonical patatin-like phospholipase A motifs, but not the nucleophilic serine, are required to mediate CapV
Q329R
phenotypes. Furthermore, CapV
Q329R
production substantially alters the lipidome and colony morphotype including rdar biofilm formation with modulation of the production of the biofilm activator CsgD, and affects additional bacterial traits such as the efficiency of phage infection and antimicrobial susceptibility. Moreover, genetically diverse commensal and pathogenic
E. coli
strains and
Salmonella typhimurium
responded with cell filamentation and modulation in colony morphotype formation to CapV
Q329R
expression. In conclusion, this work identifies the CapV variant CapV
Q329R
as a pleiotropic regulator, emphasizes a scaffold function for patatin-like phospholipases, and highlights the impact of the substitution of a single conserved amino acid for protein functionality and alteration of host physiology. |
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ISSN: | 2055-5008 2055-5008 |
DOI: | 10.1038/s41522-022-00294-z |