scholarly journals Listeria monocytogenes Possesses Adhesins for Fibronectin

1999 ◽  
Vol 67 (12) ◽  
pp. 6698-6701 ◽  
Author(s):  
Philippe Gilot ◽  
Paul André ◽  
Jean Content
Keyword(s):  
Extracellular Matrix ◽  
Listeria Monocytogenes ◽  
Cell Surface ◽  
Bacterial Cell ◽  
Cell Types ◽  
Eukaryotic Cell ◽  
Eukaryotic Cells ◽  
Food Borne ◽  
Human Fibronectin ◽  
Fibronectin Binding

ABSTRACT Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells. Several listerial surface components have been reported to interact with eukaryotic cell receptors, but the complete mechanism by which the bacteria interact with all of these cell types remains largely unknown. In this work, we found thatL. monocytogenes binds to human fibronectin, a 450,000-Da dimeric glycoprotein found in body fluids, on the surface of cells and in an insoluble component of the extracellular matrix. The binding of fibronectin to L. monocytogenes was found to be saturable and dependent on proteinaceous receptors. Five fibronectin-binding proteins of 55.3, 48.6, 46.7, 42.4, and 26.8 kDa were identified. The 55.3-kDa protein was proved to be present at the bacterial cell surface. The binding of L. monocytogenes to fibronectin adds to the number of molecules to which the bacterium is able to adhere and emphasizes the complexity of host-pathogen interactions.

scholarly journals Visualizing the dynamics of exported bacterial proteins with the chemogenetic fluorescent reporter FAST

2020 ◽  
Author(s):  
Yankel Chekli ◽  
Caroline Peron-Cane ◽  
Dario Dell’Arciprete ◽  
Jean-François Allemand ◽  
Chenge Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Listeria Monocytogenes ◽  
Cell Surface ◽  
Bacterial Cell ◽  
Surface Proteins ◽  
Cellular Functions ◽  
Reporter Protein ◽  
Cell Surface Proteins ◽  
Fluorescent Reporter ◽  
Bacterial Proteins

AbstractBacterial proteins exported to the cell surface play key cellular functions. However, despite the interest to study the localization of surface proteins such as adhesins, transporters or hydrolases, monitoring their dynamics in live imaging remains challenging, due to the limited availability of fluorescent probes remaining functional after secretion. In this work, we used the Escherichia coli intimin and the Listeria monocytogenes InlB invasin as surface exposed scaffolds fused with the recently developed chemogenetic fluorescent reporter protein FAST. Using both membrane permeant (HBR-3,5DM) and non-permeant (HBRAA-3E) fluorogens that fluoresce upon binding to FAST, we demonstrated that fully functional FAST can be exposed at the cell surface and specifically tagged on the external side of the bacterial envelop in both diderm and monoderm bacteria. Our work opens new avenues to study of the organization and dynamics of the bacterial cell surface proteins.

scholarly journals Hyaluronan Is Not a Ligand but a Regulator of Toll-Like Receptor Signaling in Mesangial Cells: Role of Extracellular Matrix in Innate Immunity

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Rainer Ebid ◽  
Julia Lichtnekert ◽  
Hans-Joachim Anders
Keyword(s):  
Extracellular Matrix ◽  
Innate Immunity ◽  
Cell Surface ◽  
Mesangial Cells ◽  
Cell Types ◽  
Dependent Manner ◽  
Glomerular Mesangial Cells ◽  
Toll Like Receptor ◽  
Surface Receptors ◽  
Tlr4 Ligand

Glomerular mesangial cells (MC), like most cell types secrete hyaluronan (HA), which attached to the cell surface via CD44, is the backbone of a hydrophilic gel matrix around these cells. Reduced extracellular matrix thickness and viscosity result from HA cleavage during inflammation. HA fragments were reported to trigger innate immunity via Toll-like receptor-(TLR-) 2 and/or TLR4 in immune cells. We questioned whether HA fragments also regulate the immunostimulatory capacity of smooth muscle cell-like MC. LPS (TLR4-ligand) and PAM3CysSK4 (TLR2-ligand) induced IL-6 secretion in MC; highly purified endotoxin-free HA < 3000 Da up to 50 μg/mL did not. Bovine-testis-hyaluronidase from was used to digest MC-HA into HA fragments of different size directly in the cell culture. Resultant HA fragments did not activate TLR4-deficient MC, while TLR2-deficient MC responded to LPS-contamination of hyaluronidase, not to produced HA fragments. Hyaluronidase increased the stimulatory effect of TLR2-/-3/-5 ligands on their TLR-receptors in TLR4-deficient MC, excluding any effect by LPS-contamination. Supplemented heparin suppressed every stimulatory effect in a dose-dependent manner. We conclude that the glycosaminoglycan HA creates a pericellular jelly barrier, which covers surface receptors like the TLRs. Barrier-thickness and viscosity balanced by HA-synthesis and degradation and the amount of HA-receptors on the cell surface regulate innate immunity via the accessibility of the receptors.

scholarly journals YscP and YscU Regulate Substrate Specificity of the Yersinia Type III Secretion System

2003 ◽  
Vol 185 (7) ◽  
pp. 2259-2266 ◽  
Author(s):  
Petra J. Edqvist ◽  
Jan Olsson ◽  
Moa Lavander ◽  
Lena Sundberg ◽  
Åke Forsberg ◽  
...  
Keyword(s):  
Cell Surface ◽  
Substrate Specificity ◽  
Type Iii Secretion ◽  
Bacterial Cell ◽  
Type Iii Secretion System ◽  
Eukaryotic Cell ◽  
Secretion System ◽  
Cell Contact ◽  
Type Iii ◽  
Bacterial Cell Surface

ABSTRACT Pathogenic Yersinia species use a type III secretion system to inhibit phagocytosis by eukaryotic cells. At 37°C, the secretion system is assembled, forming a needle-like structure on the bacterial cell surface. Upon eukaryotic cell contact, six effector proteins, called Yops, are translocated into the eukaryotic cell cytosol. Here, we show that a yscP mutant exports an increased amount of the needle component YscF to the bacterial cell surface but is unable to efficiently secrete effector Yops. Mutations in the cytoplasmic domain of the inner membrane protein YscU suppress the yscP phenotype by reducing the level of YscF secretion and increasing the level of Yop secretion. These results suggest that YscP and YscU coordinately regulate the substrate specificity of the Yersinia type III secretion system. Furthermore, we show that YscP and YscU act upstream of the cell contact sensor YopN as well as the inner gatekeeper LcrG in the pathway of substrate export regulation. These results further strengthen the strong evolutionary link between flagellar biosynthesis and type III synthesis.

scholarly journals Evidence for a role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix

1989 ◽  
Vol 262 (1) ◽  
pp. 327-334 ◽  
Author(s):  
G A Piazza ◽  
H M Callanan ◽  
J Mowery ◽  
D C Hixson
Keyword(s):  
Extracellular Matrix ◽  
Cell Surface ◽  
Rat Liver ◽  
Tissue Transglutaminase ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Type I ◽  
Cell Surface Glycoprotein ◽  
Dpp Iv ◽  
Fibronectin Binding

Dipeptidyl peptidase IV (DPP IV) is a cell surface glycoprotein which has been implicated in hepatocyte-extracellular matrix interactions [Hixson, DeLourdes, Ponce, Allison & Walborg (1984) Exp. Cell Res. 152, 402-414; Walborg, Tsuchida, Weeden, Thomas, Barrick, McEntire, Allison & Hixson (1985) Exp. Cell Res. 158, 509-518; Hanski, Huhle & Reutter (1985) Biol. Chem. Hoppe-Seyler 366, 1169-1176]. However, its proteolytic substrate(s) and/or binding protein(s) which mediate this influence have not been conclusively identified. Nitrocellulose binding assays using 125I-labelled DPP IV that was purified to homogeneity from rat hepatocytes revealed a direct interaction of DPP IV with fibronectin. Although fibronectin could mediate an indirect binding of DPP IV to collagen, no evidence was found for a direct binding of DPP IV to native or denatured Type I collagen. Fibronectin appeared to bind DPP IV at a site distinct from its exopeptidase substrate recognition site since protease inhibitors such as competitive peptide substrates and phenylmethanesulphonyl fluoride enhanced binding, possibly as a result of an altered conformation of DPP IV. To determine if fibronectin binding to DPP IV is involved in the interaction of fibronectin with the hepatocyte surface, the effect of various DPP IV inhibitors on 125I-fibronectin binding to isolated hepatocytes in suspension was examined. Kinetic studies revealed that inhibitors of DPP IV which enhanced fibronectin binding in vitro accelerated the initial binding of fibronectin to the cell surface where it was subsequently cross-linked (presumably by tissue transglutaminase) to as yet undefined components. Immunolocalization of fibronectin and DPP IV in normal rat liver sections showed that both proteins were present along the hepatocyte sinusoidal membrane. These observations, coupled with previous results showing that DPP IV is tightly bound to biomatrix isolated from rat liver (Hixson et al., 1984; Walborg et al., 1985), suggest that DPP IV binding to fibronectin may play a role in interactions of hepatocytes with extracellular matrix in vivo and possibly in matrix assembly.

scholarly journals Visualizing the dynamics of exported bacterial proteins with the chemogenetic fluorescent reporter FAST

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Yankel Chekli ◽  
Caroline Peron-Cane ◽  
Dario Dell’Arciprete ◽  
Jean-François Allemand ◽  
Chenge Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Listeria Monocytogenes ◽  
Cell Surface ◽  
Bacterial Cell ◽  
Surface Proteins ◽  
Cellular Functions ◽  
Reporter Protein ◽  
Cell Surface Proteins ◽  
Fluorescent Reporter ◽  
Bacterial Proteins

Abstract Bacterial proteins exported to the cell surface play key cellular functions. However, despite the interest to study the localisation of surface proteins such as adhesins, transporters or hydrolases, monitoring their dynamics in live imaging remains challenging, due to the limited availability of fluorescent probes remaining functional after secretion. In this work, we used the Escherichia coli intimin and the Listeria monocytogenes InlB invasin as surface exposed scaffolds fused with the recently developed chemogenetic fluorescent reporter protein FAST. Using both membrane permeant (HBR-3,5DM) and non-permeant (HBRAA-3E) fluorogens that fluoresce upon binding to FAST, we demonstrated that fully functional FAST can be exposed at the cell surface and used to specifically tag the external side of the bacterial envelop in both diderm and monoderm bacteria. Our work opens new avenues to study the organization and dynamics of the bacterial cell surface proteins.

Apoptotic Death of Listeria Monocytogenes-Infected Human Macrophages Induced by Lactoferricin B, A Bovine Lactoferrin-Derived Peptide

2005 ◽  
Vol 18 (2) ◽  
pp. 317-325 ◽  
Author(s):  
C. Longhi ◽  
M. P. Conte ◽  
S. Ranaldi ◽  
M. Penta ◽  
P. Valenti ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Bovine Milk ◽  
Cell Types ◽  
Bovine Lactoferrin ◽  
Human Macrophages ◽  
Apoptotic Death ◽  
Food Borne ◽  
Ifn Γ

Listeria monocytogenes, an intracellular facultative food-borne pathogen, was reported to induce apoptosis in vitro and in vivo in a variety of cell types with the exception of murine macrophages. These cells represent the predominant compartment of bacterial multiplication and die as a result of necrosis. In this study we showed that human non-activated and IFN-γ-activated macrophagic-like (THP-1) cells infected with L. monocytogenes, mainly die by necrosis rather than by an apoptotic process. Two natural products derived from bovine milk, lactoferrin and its derivative peptide lactoferricin B, are capable of regulating the fate of infected human macrophages. Bovine lactoferrin treatment of macrophages protects them from L. monocytogenes-induced death whereas lactoferricin B, its derivative peptide, determines a shifting of the equilibrium from necrosis to apoptosis.

Post-Golgi biosynthetic trafficking

1997 ◽  
Vol 110 (24) ◽  
pp. 3001-3009 ◽  
Author(s):  
P. Keller ◽  
K. Simons
Keyword(s):  
Cell Surface ◽  
Golgi Complex ◽  
Cell Types ◽  
Bulk Flow ◽  
Eukaryotic Cells ◽  
Flow Process ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Different Cell Types

Eukaryotic cells have developed complex machineries to distribute proteins and lipids from the Golgi complex. Contrary to what has originally been postulated, delivery of proteins to the cell surface is not a simple bulk flow process but involves sorting into distinct pathways from the trans-Golgi network. Here we describe the various routes emerging from the trans-Golgi network in different cell types, and we discuss the mechanisms that mediate sorting into these pathways. While much remains to be learned about these sorting mechanisms, it is apparent that a number of pathways previously believed to be restricted to certain cell types might be used more commonly.

scholarly journals Implication of exofacial thiol groups in the reducing activity ofListeria monocytogenes

2018 ◽  
Author(s):  
Guillaume Pillot ◽  
Anne Brillet-Viel ◽  
Hervé Prévost
Keyword(s):  
Oxidative Stress ◽  
Listeria Monocytogenes ◽  
Cell Surface ◽  
Anaerobic Condition ◽  
Bacterial Cell ◽  
Thiol Groups ◽  
Active Mechanism ◽  
Reducing Activity ◽  
Oflisteria Monocytogenes ◽  
Reduced State

AbstractListeria monocytogenesgrowing in BHI in anaerobic condition leads a decrease of redox potential at pH7 (Eh7) from 0 to −250 mV. An investigation of mechanisms involved in this reducing activity shows the implication of thiol groups located on the bacterial cell surface. Indeed, after reduction of media to −250 mV, only thiol-reactive reagents could restore the initialEh7value. Moreover, the growth ofL. monocytogenesin anaerobic condition is characterized by a reduction then acidification phases. This suggests a sensor mechanism of environmentalEh7to convert the metabolism way from the first phase to the second. Finally, the concentration of exofacial thiol still increase strongly during the acidification phase ofL. monocytogenes, even after reach the minimal value ofEh7. These results suggest that maintaining the exofacial thiol (−SH) groups in a reduced state do not depend on an active mechanism. Thiol groups appear to be displayed by membrane proteins or cell wallbound proteins and may participate in protecting cells against oxidative stress.

Attachment of Listeria monocytogenes on Ready-to-Eat Meats

2004 ◽  
Vol 67 (3) ◽  
pp. 456-462 ◽  
Author(s):  
SALLY C. C. FOONG ◽  
JAMES S. DICKSON
Keyword(s):  
Contact Angle ◽  
Listeria Monocytogenes ◽  
Cell Surface ◽  
Bacterial Cell ◽  
Negative Charge ◽  
Cell Surface Hydrophobicity ◽  
Surface Hydrophobicity ◽  
Contact Angle Measurement ◽  
Angle Measurement ◽  
Roast Beef

Five individual strains of Listeria monocytogenes and a mixed cocktail of all five were studied for attachment on frankfurters, ham, bologna, and roast beef relative to their cell surface characteristics. The ratio of strongly attached (sessile) L. monocytogenes cells compared with total (sessile and planktonic) attached cells on ready-to-eat meats was also determined. Because bacterial cell surfaces were characterized by net negative charge and hydrophobicity, electrostatic interaction chromatography and cationized ferritin methods were chosen to study net negative charge distribution on the bacterial cell surface, whereas hydrophobic interaction chromatography and contact angle measurement were used to examine the cell surface hydrophobicity. No differences (P &gt; 0.05) were observed in cell surface charge or cell surface hydrophobicity among strains. Approximately 84 to 87% L. monocytogenes were found to attach strongly to ready-to-eat meats within 5 min. No differences (P &gt; 0.05) were found among strains or among meats. Micrographs observed from scanning electron microscopy showed no differences among the strains but showed a difference in age of cells (mixed culture) in terms of surface negative charge distribution. More surface negatively charged sites were observed at 0 and 7 days and much fewer at 3 days during storage of washed, harvested cells in buffer at 4°C (aged cells under cold and nutrient deprivation), indicating a possible change in cell surface properties. Because no difference in strains was observed, the contact angle measurement study was carried out with the five-strain mixed culture. The surface hydrophobicity increased in frankfurters, decreased in roast beef, and was unchanged in ham and bologna as a result of inoculation.

scholarly journals Actin and Actin-Associated Proteins in Extracellular Vesicles Shed by Osteoclasts

2019 ◽  
Vol 21 (1) ◽  
pp. 158 ◽  
Author(s):  
L. Shannon Holliday ◽  
Lorraine Perciliano de Faria ◽  
Wellington J. Rody
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Vesicles ◽  
Active Role ◽  
Cell Types ◽  
Eukaryotic Cells ◽  
Two Dimensional ◽  
Liquid Chromatography Mass Spectrometry ◽  
Associated Proteins ◽  
Selective Incorporation ◽  
Coupling Factors

Extracellular vesicles (EVs) are shed by all eukaryotic cells and have emerged as important intercellular regulators. EVs released by osteoclasts were recently identified as important coupling factors in bone remodeling. They are shed as osteoclasts resorb bone and stimulate osteoblasts to form bone to replace the bone resorbed. We reported the proteomic content of osteoclast EVs with data from two-dimensional, high resolution liquid chromatography/mass spectrometry. In this article, we examine in detail the actin and actin-associated proteins found in osteoclast EVs. Like EVs from other cell types, actin and various actin-associated proteins were abundant. These include components of the polymerization machinery, myosin mechanoenzymes, proteins that stabilize or depolymerize microfilaments, and actin-associated proteins that are involved in regulating integrins. The selective incorporation of actin-associated proteins into osteoclast EVs suggests that they have roles in the formation of EVs and/or the regulatory signaling functions of the EVs. Regulating integrins so that they bind extracellular matrix tightly, in order to attach EVs to the extracellular matrix at specific locations in organs and tissues, is one potential active role for actin-associated proteins in EVs.

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