Recent Developments in the Interactions Between Caveolin and Pathogens

Machado, Fabiana S.; Rodríguez, Nilda E.; Adesse, Daniel; Garzoni, Luciana Ribeiro; Esper, Lísia; Lisanti, Michael P.; Burk, Robert D.; Albanese, Chris; Doorslaer, Koenraad Van; Weiss, Louis M.; Nagajyothi, Fnu; Nosanchuk, Joshua D.; Wilson, Mary E.; Tanowitz, Herbert B.

doi:10.1007/978-1-4614-1222-9_5

Cited by 28 publications

(31 citation statements)

References 124 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several pathogens and their molecules enter host cells through lipid microdomains, known as caveolae and clathrin‐coated vesicles (Machado et al, ; Moreno‐Ruiz et al, ; Rosenberger, Brumell, & Finlay, ; Veiga et al, ). To determine whether EhCP112 is being internalised into the epithelial cells by these lipid microdomains, first, MDCK cells were incubated for 1 min with rEhCP112p and then processed for TEM assays using the α‐EhCP112 antibody.…”

Section: Resultsmentioning

confidence: 99%

“…Some TEM images showed the protease in vesicles, close to the apical membranes, whereas in others, the protease appeared in vesicles inside the cell, frequently close to the intercellular space (Figure a). Caveolin‐1 and clathrin localise at membrane caveolae or clathrin‐coated vesicles, respectively, and are commonly used as markers for these structures (Machado et al, ; Veiga et al, ). To investigate whether the rEhCP112p was in caveolae or clathrin‐coated vesicles, epithelial cells were rEhCP112p‐treated and processed for immunofluorescence assays using the α‐caveolin‐1 or α‐clathrin antibodies.…”

Section: Resultsmentioning

confidence: 99%

“…In particular, T . cruzi parasitophorous vacuole colocalises with macrophages flotillin 1 and caveolin‐1 (Barrias, Dutra, De Souza, & Carvalho, ) and Leishmania chagasi colocalises with caveolin‐1 during entry (Machado et al, ). L .…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Adherens junctions and desmosomes are damaged byEntamoeba histolytica:Participation of EhCPADH complex and EhCP112 protease

Hernández-Nava

Cuellar

Nava

et al. 2017

Cellular Microbiology

View full text Add to dashboard Cite

Entamoeba histolytica trophozoites adhere to epithelium at the cell-cell contact and perturb tight junctions disturbing the transepithelial electrical resistance. Behind tight junctions are the adherens junctions (AJs) that reinforce them and the desmosomes (DSMs) that maintain the epithelium integrity. The damage produced to AJs and DMSs by this parasite is unknown. Here, we studied the effect of the trophozoites, the EhCPADH complex, and the EhCP112 recombinant enzyme (rEhCP112) on AJ and DSM proteins. We found that trophozoites degraded β-cat, E-cad, Dsp l/ll, and Dsg-2 with the participation of EhCPADH and EhCP112. After contact of epithelial cells with trophozoites, immunofluorescence and transmission electron microscopy assays revealed EhCPADH and rEhCP112 at the intercellular space where they colocalised with β-cat, E-cad, Dsp l/ll, and Dsg-2. Moreover, our results suggested that rEhCP112 could be internalised by caveolae and clathrin-coated vesicles. Immunoprecipitation assays showed the interaction of EhCPADH with β-cat and Dsp l/ll. Besides, in vivo assays demonstrated that rEhCP112 concentrates at the cellular borders of the mouse intestine degrading E-cad and Dsp I/II. Our research gives the first clues on the trophozoite attack to AJs and DSMs and point out the role of the EhCPADH and EhCP112 in the multifactorial event of trophozoites virulence.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Adherens junctions and desmosomes are damaged byEntamoeba histolytica:Participation of EhCPADH complex and EhCP112 protease

Hernández-Nava

Cuellar

Nava

et al. 2017

Cellular Microbiology

View full text Add to dashboard Cite

show abstract

“…Because caveolae do not fuse with endosomes, the internalized bacteria bypass the degradation mechanism of the host cells and remain viable within target cells (Shin and Abraham, 2001). Caveolae-mediated internalization within eukaryotic cells has been described for a number of bacteria, viruses, fungi and parasites (Machado et al, 2012). FimH-expressing E. coli, for example, has been reported to use the caveolae pathway to promote its internalization and intracellular survival within MCs (Shin et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

α-Hemolysin enhancesStaphylococcus aureusinternalization and survival within mast cells by modulating the expression of β1 integrin

Goldmann

Tuchscherr

Rohde

et al. 2016

Cellular Microbiology

View full text Add to dashboard Cite

Mast cells (MCs) are important sentinels of the host defence against invading pathogens. We previously reported that Staphylococcus aureus evaded the extracellular antimicrobial activities of MCs by promoting its internalization within these cells via β1 integrins. Here, we investigated the molecular mechanisms governing this process. We found that S. aureus responded to the antimicrobial mediators released by MCs by up-regulating the expression of α-hemolysin (Hla), fibronectin-binding protein A and several regulatory systems. We also found that S. aureus induced the up-regulation of β1 integrin expression on MCs and that this effect was mediated by Hla-ADAM10 (a disintegrin and metalloproteinase 10) interaction. Thus, deletion of Hla or inhibition of Hla-ADAM10 interaction significantly impaired S. aureus internalization within MCs. Furthermore, purified Hla but not the inactive HlaH35L induced up-regulation of β1 integrin expression in MCs in a dose-dependent manner. Our data support a model in which S. aureus counter-reacts the extracellular microbicidal mechanisms of MCs by increasing expression of fibronectin-binding proteins and by inducing Hla-ADAM10-mediated up-regulation of β1 integrin in MCs. The up-regulation of bacterial fibronectin-binding proteins, concomitantly with the increased expression of its receptor β1 integrin on the MCs, resulted in enhanced S. aureus internalization through the binding of fibronectin-binding proteins to integrin β1 via fibronectin.

show abstract

“…Recent reports on Cav1-deficient mice revealed a general enhanced susceptibility to disease provoked by local or systemic infection through certain pathogens including bacteria ( Salmonella typhimurium, Pseudomonas aeruginosa ) or parasites ( Trypanosoma cruzi ) [12], [63], [64], [65], [66], [67], [68]. Cav1-KO mice succumb to systemic infection earlier and suffer from a more severe disease phenotype than WT littermates.…”

Section: Discussionmentioning

confidence: 99%

Caveolin-1 Protects B6129 Mice against Helicobacter pylori Gastritis

et al. 2013

View full text Add to dashboard Cite

Caveolin-1 (Cav1) is a scaffold protein and pathogen receptor in the mucosa of the gastrointestinal tract. Chronic infection of gastric epithelial cells by Helicobacter pylori (H. pylori) is a major risk factor for human gastric cancer (GC) where Cav1 is frequently down-regulated. However, the function of Cav1 in H. pylori infection and pathogenesis of GC remained unknown. We show here that Cav1-deficient mice, infected for 11 months with the CagA-delivery deficient H. pylori strain SS1, developed more severe gastritis and tissue damage, including loss of parietal cells and foveolar hyperplasia, and displayed lower colonisation of the gastric mucosa than wild-type B6129 littermates. Cav1-null mice showed enhanced infiltration of macrophages and B-cells and secretion of chemokines (RANTES) but had reduced levels of CD25+ regulatory T-cells. Cav1-deficient human GC cells (AGS), infected with the CagA-delivery proficient H. pylori strain G27, were more sensitive to CagA-related cytoskeletal stress morphologies (“humming bird”) compared to AGS cells stably transfected with Cav1 (AGS/Cav1). Infection of AGS/Cav1 cells triggered the recruitment of p120 RhoGTPase-activating protein/deleted in liver cancer-1 (p120RhoGAP/DLC1) to Cav1 and counteracted CagA-induced cytoskeletal rearrangements. In human GC cell lines (MKN45, N87) and mouse stomach tissue, H. pylori down-regulated endogenous expression of Cav1 independently of CagA. Mechanistically, H. pylori activated sterol-responsive element-binding protein-1 (SREBP1) to repress transcription of the human Cav1 gene from sterol-responsive elements (SREs) in the proximal Cav1 promoter. These data suggested a protective role of Cav1 against H. pylori-induced inflammation and tissue damage. We propose that H. pylori exploits down-regulation of Cav1 to subvert the host's immune response and to promote signalling of its virulence factors in host cells.

show abstract

Recent Developments in the Interactions Between Caveolin and Pathogens

Cited by 28 publications

References 124 publications

Adherens junctions and desmosomes are damaged byEntamoeba histolytica:Participation of EhCPADH complex and EhCP112 protease

Adherens junctions and desmosomes are damaged byEntamoeba histolytica:Participation of EhCPADH complex and EhCP112 protease

α-Hemolysin enhancesStaphylococcus aureusinternalization and survival within mast cells by modulating the expression of β1 integrin

Caveolin-1 Protects B6129 Mice against Helicobacter pylori Gastritis

Contact Info

Product

Resources

About