scholarly journals Porphyromonas gingivalis induces penetration of lipopolysaccharide and peptidoglycan through the gingival epithelium via degradation of coxsackievirus and adenovirus receptor

2021 ◽  
Author(s):  
Hiroki Takeuchi ◽  
Shunsuke Yamaga ◽  
Naoko Sasaki ◽  
Masae Kuboniwa ◽  
Michiya Matsusaki ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Three Dimensional ◽  
Protein S ◽  
Cysteine Proteases ◽  
Epithelial Barrier ◽  
Epithelial Tissue ◽  
Central Feature ◽  
Tissue Model ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor

Abstract Porphyromonas gingivalis is a major pathogen in severe and chronic manifestations of periodontal disease, which is one of the most common infections of humans. A central feature of P. gingivalis pathogenicity is dysregulation of innate immunity at the gingival epithelial interface. We previously showed that junctional adhesion molecule 1 (JAM1) was specifically degraded by P. gingivalis, leading to epithelial barrier breakdown in gingival tissues. Whereas, the involvement of the other JAM family protein(s) in the epithelial barrier dysregulation by P. gingivalis remains unknown. Here we show that Arg-specific or Lys-specific cysteine proteases named gingipains produced by P. gingivalis specifically degrade coxsackievirus and adenovirus receptor (CXADR), a tight junction associated protein, at R145 and K235 in gingival epithelial cells. A P. gingivalis strain lacking gingipains was impaired in degradation of CXADR. Knockdown of CXADR in a three-dimensional multilayered tissue model increased permeability to 40 kDa dextran, lipopolysaccharide, and proteoglycan. Inversely, overexpression of CXADR in a gingival epithelial tissue model prevented penetration by these agents following P. gingivalis infection. Our findings strongly suggest that P. gingivalis gingipains disrupt barrier function of stratified squamous epithelium via degradation of CXADR as well as JAM1, efficiently allowing bacterial virulence factors to penetrate into subepithelial tissues.

scholarly journals Effects of a tart cherry (Prunus cerasus L.) phenolic extract on Porphyromonas gingivalis and its ability to impair the oral epithelial barrier

PLoS ONE ◽  
2021 ◽  
Vol 16 (1) ◽  
pp. e0246194
Author(s):  
Amel Ben Lagha ◽  
Geneviève Pellerin ◽  
Katy Vaillancourt ◽  
Daniel Grenier
Keyword(s):  
Protective Effect ◽  
Porphyromonas Gingivalis ◽  
Periodontal Diseases ◽  
Cysteine Proteases ◽  
Prunus Cerasus ◽  
Epithelial Barrier ◽  
Tart Cherry ◽  
Phenolic Extract ◽  
Oral Epithelial

Periodontal diseases, including gingivitis and periodontitis, are a global oral health problem. Porphyromonas gingivalis, a key pathogen involved in the onset of periodontitis, is able to colonize the subgingival epithelium and invade the underlying connective tissue due to the contribution of cysteine proteases known as gingipains. In this study, we investigated the effects of a phenolic extract prepared from tart cherry (Prunus cerasus L.) juice on the growth, adherence, and protease activity of P. gingivalis. We also assessed the protective effect of the tart cherry extract on the disruption of the oral epithelial barrier induced by P. gingivalis. The tart cherry extract that contains procyanidins and quercetin and its derivatives (rutinoside, glucoside) as the most important phenolic compounds attenuated P. gingivalis growth, reduced adherence to an experimental basement membrane matrix model, and decreased the protease activities of P. gingivalis. The tart cherry extract also exerted a protective effect on the integrity of the oral epithelial barrier in an in vitro model infected with P. gingivalis. More specifically, the extract prevented a decrease in transepithelial electrical resistance as well as the destruction of tight junction proteins (zonula occludens-1 and occludin). These results suggest that the tart cherry phenolic extract may be a promising natural product for the treatment of periodontitis through its ability to attenuate the virulence properties of P. gingivalis and curtail the ability of this pathogen to impair the oral epithelial barrier.

Projected Structure of the Surface Protein of Sulfolobus Spec. B12 Determined to a Resolution of 1.0 NM by Cryo-Electronmicroscopy

1990 ◽  
Vol 48 (1) ◽  
pp. 102-103
Author(s):  
G. Lembcke ◽  
F. Zemlin
Keyword(s):  
Low Dose ◽  
Maximum Dose ◽  
Three Dimensional ◽  
Surface Protein ◽  
Protein S ◽  
Radiation Sensitivity ◽  
Specimen Preparation ◽  
Molecular Architecture ◽  
High Radiation ◽  
Fritz Haber

The thermoacidophilic archaebacterium Sulfolobus spec. B12 , which is closely related to Sulfolobus solfataricus , possesses a regularly arrayed surface protein (S-layer), which is linked to the plasma membrane via spacer elements spanning a distinct interspace of approximately 18 nm. The S-layer has p3-Symmetry and a lattice constant of 21 nm; three-dimensional reconstructions of negatively stained fragments yield a layer thickness of approximately 6-7 nm.For analysing the molecular architecture of Sulfolobus surface protein in greater detail we use aurothioglucose(ATG)-embedding for specimen preparation. Like glucose, ATG, is supposed to mimic the effect of water, but has the advantage of being less volatile. ATG has advantages over glucose when working with specimens composed exclusively of protein because of its higher density of 2.92 g cm-3. Because of its high radiation sensitivity electromicrographs has to be recorded under strict low-dose conditions. We have recorded electromicrographs with a liquid helium-cooled superconducting electron microscope (the socalled SULEIKA at the Fritz-Haber-lnstitut) with a specimen temperature of 4.5 K and with a maximum dose of 2000 e nm-2 avoiding any pre-irradiation of the specimen.

scholarly journals Development of a human neuromuscular tissue-on-a-chip model on a 24-well-plate-format compartmentalized microfluidic device

Lab on a Chip ◽  
2021 ◽  
Author(s):  
Kazuki Yamamoto ◽  
Nao Yamaoka ◽  
Yu Imaizumi ◽  
Takunori Nagashima ◽  
Taiki Furutani ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Microfluidic Device ◽  
Motor Neurons ◽  
Muscle Fibers ◽  
Three Dimensional ◽  
Tissue Model ◽  
Skeletal Muscle Fibers

A three-dimensional human neuromuscular tissue model that mimics the physically separated structures of motor neurons and skeletal muscle fibers is presented.

scholarly journals The Coxsackievirus and Adenovirus Receptor: Glycosylation and the Extracellular D2 Domain Are Not Required for Coxsackievirus B3 Infection

2016 ◽  
Vol 90 (12) ◽  
pp. 5601-5610 ◽  
Author(s):  
Sandra Pinkert ◽  
Carsten Röger ◽  
Jens Kurreck ◽  
Jeffrey M. Bergelson ◽  
Henry Fechner
Keyword(s):  
Virus Infection ◽  
Immunoglobulin Superfamily ◽  
Minor Importance ◽  
Receptor Function ◽  
Virus Binding ◽  
D2 Domain ◽  
Cvb3 Infection ◽  
Coxsackie B Viruses ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor

ABSTRACTThe coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin superfamily (IgSF) and functions as a receptor for coxsackie B viruses (CVBs). The extracellular portion of CAR comprises two glycosylated immunoglobulin-like domains, D1 and D2. CAR-D1 binds to the virus and is essential for virus infection; however, it is not known whether D2 is also important for infection, and the role of glycosylation has not been explored. To understand the function of these structural components in CAR-mediated CVB3 infection, we generated a panel of human (h) CAR deletion and substitution mutants and analyzed their functionality as CVB receptors, examining both virus binding and replication. Lack of glycosylation of the CAR-D1 or -D2 domains did not adversely affect CVB3 binding or infection, indicating that the glycosylation of CAR is not required for its receptor functions. Deletion of the D2 domain reduced CVB3 binding, with a proportionate reduction in the efficiency of virus infection. Replacement of D2 with the homologous D2 domain from chicken CAR, or with the heterologous type C2 immunoglobulin-like domain from IgSF11, another IgSF member, fully restored receptor function; however, replacement of CAR-D2 with domains from CD155 or CD80 restored function only in part. These data indicate that glycosylation of the extracellular domain of hCAR plays no role in CVB3 receptor function and that CAR-D2 is not specifically required. The D2 domain may function largely as a spacer permitting virus access to D1; however, the data may also suggest that D2 affects virus binding by influencing the conformation of D1.IMPORTANCEAn important step in virus infection is the initial interaction of the virus with its cellular receptor. Although the role in infection of the extracellular CAR-D1, cytoplasmic, and transmembrane domains have been analyzed extensively, nothing is known about the function of CAR-D2 and the extracellular glycosylation of CAR. Our data indicate that glycosylation of the extracellular CAR domain has only minor importance for the function of CAR as CVB3 receptor and that the D2 domain is not essential per se but contributes to receptor function by promoting the exposure of the D1 domain on the cell surface. These results contribute to our understanding of the coxsackievirus-receptor interactions.

Application of combined three-dimensional bone and soft tissue model

1998 ◽  
Vol 27 (6) ◽  
pp. 482-484 ◽  
Author(s):  
Gert Santler ◽  
Hans Kaercher ◽  
Alexander Gaggl ◽  
Guenter Schultes
Keyword(s):  
Soft Tissue ◽  
Three Dimensional ◽  
Tissue Model

Evaluation of photodynamic therapy efficiency using an in vitro three-dimensional microfluidic breast cancer tissue model

Lab on a Chip ◽  
2015 ◽  
Vol 15 (3) ◽  
pp. 735-744 ◽  
Author(s):  
Yamin Yang ◽  
Xiaochuan Yang ◽  
Jin Zou ◽  
Chao Jia ◽  
Yue Hu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Gold Nanoparticles ◽  
Photodynamic Therapy ◽  
Three Dimensional ◽  
Therapeutic Agents ◽  
Breast Cancer Tissue ◽  
Cancer Tissue ◽  
Tissue Model

A microfluidic-based in vitro three-dimensional (3D) breast cancer tissue model was established for determining the efficiency of photodynamic therapy (PDT) with therapeutic agents (photosensitizer and gold nanoparticles) under various irradiation conditions.

Three-dimensional tissue model in direct contact with an on-chip vascular bed enabled by removable membranes

Lab on a Chip ◽  
2022 ◽  
Author(s):  
Yoshikazu Kameda ◽  
Surachada Chuaychob ◽  
Miwa Tanaka ◽  
Yang Liu ◽  
Ryu Okada ◽  
...  
Keyword(s):  
Tissue Culture ◽  
Direct Contact ◽  
Three Dimensional ◽  
Culture Period ◽  
Tissue Model ◽  
Vascular Bed ◽  
On Chip

Three-dimensional (3D) tissue culture is a powerful tool for understanding physiological events. However, 3D tissues still have limitations in their size, culture period, and maturity, which are caused by the...

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