ArticleOpen biology2016
The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Genomic insights into Shigella species isolated from small ruminants and manure in the North West Province, South Africa.Applied microbiology and biotechnology · 2025Article
- Identification and characterisation of a major outer membrane protein from Methylacidiphilum fumariolicum SolV.Antonie van Leeuwenhoek · 2023Article
- Shigella Outer Membrane Vesicles as Promising Targets for Vaccination.International journal of molecular sciences · 2022Review
- Gene Transfer Potential of Outer Membrane Vesicles of Gram-Negative Bacteria.International journal of molecular sciences · 2021Review
- A Coxiella burnetii phospholipase A homolog pldA is required for optimal growth in macrophages and developmental form lipid remodeling.BMC microbiology · 2018Article
- Proteomics, Bioinformatics and Structure-Function Antigen Mining For Gonorrhea Vaccines.Frontiers in immunology · 2018Review
- Outer membrane phospholipase A's roles inGut pathogens · 2017Article
- Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Outer membrane phospholipase A (OMPLA) is an enzyme located in the outer membrane of Gram-negative bacteria. OMPLA exhibits broad substrate specificity, and some of its substrates are located in the cellular envelope. Generally, the enzymatic activity can only be induced by perturbation of the cell envelope integrity through diverse methods. Although OMPLA has been thoroughly studied as a membrane protein in Escherichia coli and is constitutively expressed in many other bacterial pathogens, little is known regarding the functions of OMPLA during the process of bacterial infection. In this study, the proteomic and transcriptomic data indicated that OMPLA in Shigella flexneri, termed PldA, both stabilizes the bacterial membrane and is involved in bacterial infection under ordinary culture conditions. A series of physiological assays substantiated the disorganization of the bacterial outer membrane and the periplasmic space in the ΔpldA mutant strain. Furthermore, the ΔpldA mutant strain showed decreased levels of type III secretion system expression, contributing to the reduced internalization efficiency in host cells. The results of this study support that PldA, which is widespread across Gram-negative bacteria, is an important factor for the bacterial life cycle, particularly in human pathogens.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.