Encoding for a Fructose Specific PTS Permease IIA May Be Required for Virulence in Strain F2365.

Front Microbiol

Residue Chemistry and Predictive Microbiology Research Unit, Eastern Regional Research Center, Agricultural Research Service, United States Department of Agriculture, WyndmoorPA, United States.

Published: August 2017

is a foodborne pathogen that causes listeriosis, which is a major public health concern due to the high fatality rate. , and encode for fructose-specific EIIABC components of phosphotransferase transport system (PTS) permease that is responsible for sugar transport. In previous studies, in-frame deletion mutants of a putative fructose-specific PTS permease (, and ) were constructed and analyzed. However, the virulence potential of these deletion mutants has not been studied. In this study, two methods were used to analyze the virulence potential of these deletion mutants. First, invasion assays were used to measure the invasion efficiencies to host cells using the human HT-29 cell line. Second, plaque forming assays were used to measure cell-to-cell spread in host cells. Our results showed that the deletion mutant Δ had reduced invasion and cell-to-cell spread efficiencies in human cell line compared to the parental strain , indicating that encoding for a fructose specific PTS permease IIA may be required for virulence in strain F2365. In addition, the gene expression levels of 15 virulence and stress-related genes were analyzed in the stationary phase cells of the deletion mutants using RT-PCR assays. Virulence-related gene expression levels were elevated in the deletion mutants Δ compared to the wild type parental strain , indicating the down-regulation of virulence genes by this PTS permease in . Finally, stress-related gene expression levels were also increased in all of the deletion mutants, suggesting the involvement of this PTS permease in stress response. Furthermore, these deletion mutants displayed the same pressure tolerance and the same capacity for biofilm formation compared to the wild-type parental strain . In summary, our findings suggest that the gene can be used as a potential target to develop inhibitors for new therapeutic and pathogen control strategies for public health.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5581801PMC
http://dx.doi.org/10.3389/fmicb.2017.01611DOI Listing

Publication Analysis

Top Keywords

deletion mutants
28
pts permease
24
parental strain
12
gene expression
12
expression levels
12
encoding fructose
8
fructose specific
8
specific pts
8
permease iia
8
iia required
8

Similar Publications

is a Gram-negative bacterium and human pathogen that is linked to various gastric diseases, including peptic ulcer disease, chronic gastritis, and gastric cancer. The filament of the flagellum is surrounded by a membranous sheath that is contiguous with the outer membrane. Proteomic analysis of isolated sheathed flagella from B128 identified the lipoprotein HP0135 as a potential component of the flagellar sheath.

View Article and Find Full Text PDF

We analyzed the transcriptome data of wildtype and estrogen receptor β knockout () rat ovaries during the early postnatal period and detected remarkable changes in epigenetic regulators and transcription factors. Compared with postnatal day (PD) 4.5 ovaries, PD 6.

View Article and Find Full Text PDF

Structure-Function Relationship of the β-Hairpin of HB27 Laccase.

Int J Mol Sci

January 2025

Departamento de Micro y Nanotecnologías, Instituto de Ciencias Aplicadas y Tecnología, Universidad Nacional Autónoma de México, Cto. Exterior S/N, C.U., Coyoacán, Ciudad de México C.P. 04510, Mexico.

Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) and one with a partially modified β-hairpin (P1Tth-Lac). Enzymatic activity was assayed with different substrates with and without copper.

View Article and Find Full Text PDF

Sequences and three-dimensional structures of the four vertebrate arrestins are very similar, yet in sharp contrast to other subtypes, arrestin-1 demonstrates exquisite selectivity for the active phosphorylated form of its cognate receptor, rhodopsin. The N-terminus participates in receptor binding and serves as the anchor of the C-terminus, the release of which facilitates arrestin transition into a receptor-binding state. We tested the effects of substitutions of fourteen residues in the N-terminus of arrestin-1 on the binding to phosphorylated and unphosphorylated light-activated rhodopsin of wild-type protein and its enhanced mutant with C-terminal deletion that demonstrates higher binding to both functional forms of rhodopsin.

View Article and Find Full Text PDF

AcfA Regulates the Virulence and Cell Envelope Stress Response of .

Microorganisms

December 2024

School of Food Science and Engineering, Shaanxi University of Science & Technology, No. 6 Xuefu Road, Xi'an 710021, China.

is a ubiquitous inhabitant of estuarine and marine environments that causes vibriosis in aquatic animals and food poisoning in humans. Accessory colonizing factor (ACF) is employed by to assist in the colonization and invasion of host cells leading to subsequent illnesses. In this work, Δ, an in-frame deletion mutant strain lacking the 4th to the 645th nucleotides of the open reading frame (ORF) of the gene, and the complementary strain were constructed to decipher the function of AcfA in .

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!