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Article ; Online: Structural insights into hepatitis C virus neutralization.

Ströh, Luisa J / Krey, Thomas

2023 Volume 60, Page(s) 101316

Abstract: Inspite of the available antiviral therapy, hepatitis C virus (HCV) remains a global health burden and a prophylactic vaccine would help to eliminate the risk to develop chronic liver diseases. Structural insights into the function of the glycoproteins ... ...

Abstract	Inspite of the available antiviral therapy, hepatitis C virus (HCV) remains a global health burden and a prophylactic vaccine would help to eliminate the risk to develop chronic liver diseases. Structural insights into the function of the glycoproteins E1 and E2 in virus entry and the interplay with the host's humoral immune response are key for informed vaccine development. We review recently reported structural insights into receptor binding of HCV glycoproteins and the assembly of an intact membrane-bound E1-E2 heterodimer. These data are used together with available functional data to draw a simplified model of virus entry, which highlights gaps in our current knowledge that warrant further research to fully understand this process at the atomic level.
MeSH term(s)	Humans ; Hepacivirus ; Hepatitis C ; Protein Binding ; Viral Envelope Proteins/metabolism
Chemical Substances	Viral Envelope Proteins
Language	English
Publishing date	2023-03-29
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2611378-8
ISSN	1879-6265 ; 1879-6257
ISSN (online)	1879-6265
ISSN	1879-6257
DOI	10.1016/j.coviro.2023.101316
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Article ; Online: HCV Glycoprotein Structure and Implications for B-Cell Vaccine Development.

Ströh, Luisa J / Krey, Thomas

International journal of molecular sciences

2020 Volume 21, Issue 18

Abstract: Despite the approval of highly efficient direct-acting antivirals in the last decade Hepatitis C virus (HCV) remains a global health burden and the development of a vaccine would constitute an important step towards the control of HCV. The high genetic ... ...

Abstract	Despite the approval of highly efficient direct-acting antivirals in the last decade Hepatitis C virus (HCV) remains a global health burden and the development of a vaccine would constitute an important step towards the control of HCV. The high genetic variability of the viral glycoproteins E1 and E2, which carry the main neutralizing determinants, together with their intrinsic structural flexibility, the high level of glycosylation that shields conserved neutralization epitopes and immune evasion using decoy epitopes renders the design of an efficient vaccine challenging. Recent structural and functional analyses have highlighted the role of the CD81 receptor binding site on E2, which overlaps with those neutralization epitopes within E2 that have been structurally characterized to date. This CD81 binding site consists of three distinct segments including "epitope I", "epitope II" and the "CD81 binding loop". In this review we summarize the structural features of the HCV glycoproteins that have been derived from X-ray structures of neutralizing and non-neutralizing antibody fragments complexed with either recombinant E2 or epitope-derived linear peptides. We focus on the current understanding how neutralizing antibodies interact with their cognate antigen, the structural features of the respective neutralization epitopes targeted by nAbs and discuss the implications for informed vaccine design.
MeSH term(s)	Antibodies, Neutralizing/immunology ; Antigen-Antibody Reactions ; Antigens, Viral/chemistry ; Antigens, Viral/immunology ; B-Lymphocytes/immunology ; Dimerization ; Epitopes/chemistry ; Epitopes/immunology ; Glycosylation ; Hepacivirus/chemistry ; Hepacivirus/immunology ; Hepatitis C Antibodies/immunology ; Humans ; Immunoglobulin Fab Fragments/immunology ; Models, Molecular ; Peptide Fragments/chemical synthesis ; Peptide Fragments/chemistry ; Peptide Fragments/immunology ; Protein Conformation ; Protein Domains ; Protein Processing, Post-Translational ; Single-Chain Antibodies/immunology ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/immunology ; Viral Hepatitis Vaccines
Chemical Substances	Antibodies, Neutralizing ; Antigens, Viral ; E1 protein, Hepatitis C virus ; Epitopes ; Hepatitis C Antibodies ; Immunoglobulin Fab Fragments ; Peptide Fragments ; Single-Chain Antibodies ; Viral Envelope Proteins ; Viral Hepatitis Vaccines ; glycoprotein E2, Hepatitis C virus (157184-61-7)
Language	English
Publishing date	2020-09-16
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21186781
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Article: Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.

Ströh, Luisa J / Nagarathinam, Kumar / Krey, Thomas

Frontiers in immunology

2018 Volume 9, Page(s) 1396

Abstract: Numerous antibodies have been described that potently neutralize a broad range of hepatitis C virus (HCV) isolates and the majority of these antibodies target the binding site for the cellular receptor CD81 within the major HCV glycoprotein E2. A ... ...

Abstract	Numerous antibodies have been described that potently neutralize a broad range of hepatitis C virus (HCV) isolates and the majority of these antibodies target the binding site for the cellular receptor CD81 within the major HCV glycoprotein E2. A detailed understanding of the major antigenic determinants is crucial for the design of an efficient vaccine that elicits high levels of such antibodies. In the past 6 years, structural studies have shed additional light on the way the host's humoral immune system recognizes neutralization epitopes within the HCV glycoproteins. One of the most striking findings from these studies is that the same segments of the E2 polypeptide chain induce antibodies targeting distinct antigen conformations. This was demonstrated by several crystal structures of identical polypeptide segments bound to different antibodies, highlighting an unanticipated intrinsic structural flexibility that allows binding of antibodies with distinct paratope shapes following an "induced-fit" mechanism. This unprecedented flexibility extends to the entire binding site for the cellular receptor CD81, underlining the importance of dynamic analyses to understand (1) the interplay between HCV and the humoral immune system and (2) the relevance of this structural flexibility for virus entry. This review summarizes the current understanding how neutralizing antibodies target structurally flexible epitopes. We focus on differences and common features of the reported structures and discuss the implications of the observed structural flexibility for the viral replication cycle, the full scope of the interplay between the virus and the host immune system and-most importantly-informed vaccine design.
Language	English
Publishing date	2018
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2606827-8
ISSN	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2018.01396
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Article: Glycan Engagement by Viruses: Receptor Switches and Specificity.

Ströh, Luisa J / Stehle, Thilo

Annual review of virology

2014 Volume 1, Issue 1, Page(s) 285–306

Abstract: A large number of viruses, including many human pathogens, bind cell-surface glycans during the initial steps of infection. Viral glycan receptors such as glycosaminoglycans and sialic acid-containing carbohydrates are often negatively charged, but ... ...

Abstract	A large number of viruses, including many human pathogens, bind cell-surface glycans during the initial steps of infection. Viral glycan receptors such as glycosaminoglycans and sialic acid-containing carbohydrates are often negatively charged, but neutral glycans such as histo-blood group antigens can also function as receptors. The engagement of glycans facilitates attachment and entry and, consequently, is often a key determinant of the host range, tissue tropism, pathogenicity, and transmissibility of viruses. Here, we review current knowledge about virus-glycan interactions using representative crystal structures of viral attachment proteins in complex with glycans. We illuminate the determinants of specificity utilized by different glycan-binding viruses and explore the potential of these interactions for switching receptor specificities within or even between glycan classes. A detailed understanding of these parameters is important for the prediction of binding sites where structural information is not available, and is invaluable for the development of antiviral therapeutics.
Language	English
Publishing date	2014-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	2764224-0
ISSN	2327-0578 ; 2327-056X
ISSN (online)	2327-0578
ISSN	2327-056X
DOI	10.1146/annurev-virology-031413-085417
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Article ; Online: Viral Glycoproteins Induce NLRP3 Inflammasome Activation and Pyroptosis in Macrophages.

Eisfeld, Hannah S / Simonis, Alexander / Winter, Sandra / Chhen, Jason / Ströh, Luisa J / Krey, Thomas / Koch, Manuel / Theobald, Sebastian J / Rybniker, Jan

Viruses

2021 Volume 13, Issue 10

Abstract: Infections with viral pathogens are widespread and can cause a variety of different diseases. In-depth knowledge about viral triggers initiating an immune response is necessary to decipher viral pathogenesis. Inflammasomes, as part of the innate immune ... ...

Abstract	Infections with viral pathogens are widespread and can cause a variety of different diseases. In-depth knowledge about viral triggers initiating an immune response is necessary to decipher viral pathogenesis. Inflammasomes, as part of the innate immune system, can be activated by viral pathogens. However, viral structural components responsible for inflammasome activation remain largely unknown. Here we analyzed glycoproteins derived from SARS-CoV-1/2, HCMV and HCV, required for viral entry and fusion, as potential triggers of NLRP3 inflammasome activation and pyroptosis in THP-1 macrophages. All tested glycoproteins were able to potently induce NLRP3 inflammasome activation, indicated by ASC-SPECK formation and secretion of cleaved IL-1β. Lytic cell death via gasdermin D (GSDMD), pore formation, and pyroptosis are required for IL-1β release. As a hallmark of pyroptosis, we were able to detect cleavage of GSDMD and, correspondingly, cell death in THP-1 macrophages. CRISPR-Cas9 knockout of NLRP3 and GSDMD in THP-1 macrophages confirmed and strongly support the evidence that viral glycoproteins can act as innate immunity triggers. With our study, we decipher key mechanisms of viral pathogenesis by showing that viral glycoproteins potently induce innate immune responses. These insights could be beneficial in vaccine development and provide new impulses for the investigation of vaccine-induced innate immunity.
MeSH term(s)	Cell Line, Tumor ; Cytomegalovirus/immunology ; Hepacivirus/immunology ; Humans ; Immunity, Innate/immunology ; Inflammasomes/immunology ; Interleukin-1beta/biosynthesis ; Interleukin-1beta/immunology ; Macrophages/immunology ; NLR Family, Pyrin Domain-Containing 3 Protein/immunology ; Pyroptosis/immunology ; SARS Virus/immunology ; SARS-CoV-2/immunology ; THP-1 Cells ; Viral Envelope Proteins/immunology ; Viral Fusion Proteins/immunology
Chemical Substances	IL1B protein, human ; Inflammasomes ; Interleukin-1beta ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; Viral Envelope Proteins ; Viral Fusion Proteins
Language	English
Publishing date	2021-10-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13102076
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Article: Viral Glycoproteins Induce NLRP3 Inflammasome Activation and Pyroptosis in Macrophages

Eisfeld, Hannah S. / Simonis, Alexander / Winter, Sandra / Chhen, Jason / Ströh, Luisa J. / Krey, Thomas / Koch, Manuel / Theobald, Sebastian J. / Rybniker, Jan

Viruses. 2021 Oct. 15, v. 13, no. 10

2021

Abstract	Infections with viral pathogens are widespread and can cause a variety of different diseases. In-depth knowledge about viral triggers initiating an immune response is necessary to decipher viral pathogenesis. Inflammasomes, as part of the innate immune system, can be activated by viral pathogens. However, viral structural components responsible for inflammasome activation remain largely unknown. Here we analyzed glycoproteins derived from SARS-CoV-1/2, HCMV and HCV, required for viral entry and fusion, as potential triggers of NLRP3 inflammasome activation and pyroptosis in THP-1 macrophages. All tested glycoproteins were able to potently induce NLRP3 inflammasome activation, indicated by ASC-SPECK formation and secretion of cleaved IL-1β. Lytic cell death via gasdermin D (GSDMD), pore formation, and pyroptosis are required for IL-1β release. As a hallmark of pyroptosis, we were able to detect cleavage of GSDMD and, correspondingly, cell death in THP-1 macrophages. CRISPR-Cas9 knockout of NLRP3 and GSDMD in THP-1 macrophages confirmed and strongly support the evidence that viral glycoproteins can act as innate immunity triggers. With our study, we decipher key mechanisms of viral pathogenesis by showing that viral glycoproteins potently induce innate immune responses. These insights could be beneficial in vaccine development and provide new impulses for the investigation of vaccine-induced innate immunity.
Keywords	CRISPR-Cas systems ; glycoproteins ; immune response ; inflammasomes ; innate immunity ; macrophages ; pathogenesis ; pyroptosis ; secretion ; vaccine development
Language	English
Dates of publication	2021-1015
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v13102076
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Structural Basis and Evolution of Glycan Receptor Specificities within the Polyomavirus Family.

Ströh, Luisa J / Rustmeier, Nils H / Blaum, Bärbel S / Botsch, Josephine / Rößler, Philip / Wedekink, Florian / Lipkin, W Ian / Mishra, Nischay / Stehle, Thilo

mBio

2020 Volume 11, Issue 4

Abstract: Asymptomatic infections with polyomaviruses in humans are common, but these small viruses can cause severe diseases in immunocompromised hosts. New Jersey polyomavirus (NJPyV) was identified via a muscle biopsy in an organ transplant recipient with ... ...

Abstract	Asymptomatic infections with polyomaviruses in humans are common, but these small viruses can cause severe diseases in immunocompromised hosts. New Jersey polyomavirus (NJPyV) was identified via a muscle biopsy in an organ transplant recipient with systemic vasculitis, myositis, and retinal blindness, and human polyomavirus 12 (HPyV12) was detected in human liver tissue. The evolutionary origins and potential diseases are not well understood for either virus. In order to define their receptor engagement strategies, we first used nuclear magnetic resonance (NMR) spectroscopy to establish that the major capsid proteins (VP1) of both viruses bind to sialic acid in solution. We then solved crystal structures of NJPyV and HPyV12 VP1 alone and in complex with sialylated glycans. NJPyV employs a novel binding site for a α2,3-linked sialic acid, whereas HPyV12 engages terminal α2,3- or α2,6-linked sialic acids in an exposed site similar to that found in
Language	English
Publishing date	2020-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.00745-20
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Article ; Online: Global and local envelope protein dynamics of hepatitis C virus determine broad antibody sensitivity.

Augestad, Elias H / Castelli, Matteo / Clementi, Nicola / Ströh, Luisa J / Krey, Thomas / Burioni, Roberto / Mancini, Nicasio / Bukh, Jens / Prentoe, Jannick

Science advances

2020 Volume 6, Issue 35, Page(s) eabb5938

Abstract: Broad antibody sensitivity differences of hepatitis C virus (HCV) isolates and their ability to persist in the presence of neutralizing antibodies (NAbs) remain poorly understood. Here, we show that polymorphisms within glycoprotein E2, including ... ...

Abstract	Broad antibody sensitivity differences of hepatitis C virus (HCV) isolates and their ability to persist in the presence of neutralizing antibodies (NAbs) remain poorly understood. Here, we show that polymorphisms within glycoprotein E2, including hypervariable region 1 (HVR1) and antigenic site 412 (AS412), broadly affect NAb sensitivity by shifting global envelope protein conformation dynamics between theoretical "closed," neutralization-resistant and "open," neutralization-sensitive states. The conformational space of AS412 was skewed toward β-hairpin-like conformations in closed states, which also depended on HVR1, assigning function to these enigmatic E2 regions. Scavenger receptor class B, type I entry dependency of HCV was associated with NAb resistance and correlated perfectly with decreased virus propensity to interact with HCV co-receptor CD81, indicating that decreased NAb sensitivity resulted in a more complex entry pathway. This link between global E1/E2 states and functionally distinct AS412 conformations has important implications for targeting AS412 in rational HCV vaccine designs.
MeSH term(s)	Antibodies, Neutralizing ; Hepacivirus/genetics ; Hepatitis C ; Hepatitis C Antibodies ; Humans ; Viral Envelope Proteins/metabolism
Chemical Substances	Antibodies, Neutralizing ; Hepatitis C Antibodies ; Viral Envelope Proteins
Language	English
Publishing date	2020-08-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abb5938
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Article ; Online: Single-nucleotide variants in human CD81 influence hepatitis C virus infection of hepatoma cells.

Alberione, María Pía / Moeller, Rebecca / Kirui, Jared / Ginkel, Corinne / Doepke, Mandy / Ströh, Luisa J / Machtens, Jan-Philipp / Pietschmann, Thomas / Gerold, Gisa

Medical microbiology and immunology

2020 Volume 209, Issue 4, Page(s) 499–514

Abstract: An estimated number of 71 million people are living with chronic hepatitis C virus (HCV) infection worldwide and 400,000 annual deaths are related to the infection. HCV entry into the hepatocytes is complex and involves several host factors. The ... ...

Abstract	An estimated number of 71 million people are living with chronic hepatitis C virus (HCV) infection worldwide and 400,000 annual deaths are related to the infection. HCV entry into the hepatocytes is complex and involves several host factors. The tetraspanin human CD81 (hCD81) is one of the four essential entry factors and is composed of one large extracellular loop, one small extracellular loop, four transmembrane domains, one intracellular loop and two intracellular tails. The large extracellular loop interacts with the E2 glycoprotein of HCV. Regions outside the large extracellular loop (backbone) of hCD81 have a critical role in post-binding entry steps and determine susceptibility of hepatocytes to HCV. Here, we investigated the effect of five non-synonymous single-nucleotide variants in the backbone of hCD81 on HCV susceptibility. We generated cell lines that stably express the hCD81 variants and infected the cells using HCV pseudoparticles and cell culture-derived HCV. Our results show that all the tested hCD81 variants support HCV pseudoparticle entry with similar efficiency as wild-type hCD81. In contrast, variants A54V, V211M and M220I are less supportive to cell culture-derived HCV infection. This altered susceptibility is HCV genotype dependent and specifically affected the cell entry step. Our findings identify three hCD81 genetic variants that are impaired in their function as HCV host factors for specific viral genotypes. This study provides additional evidence that genetic host variation contributes to inter-individual differences in HCV infection and outcome.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Cell Line, Tumor/virology ; HEK293 Cells/virology ; Hepatitis C, Chronic/metabolism ; Hepatocytes/metabolism ; Hepatocytes/virology ; Humans ; Point Mutation ; Tetraspanin 28/genetics ; Tetraspanin 28/metabolism ; Viral Envelope Proteins/metabolism ; Virus Internalization
Chemical Substances	CD81 protein, human ; Tetraspanin 28 ; Viral Envelope Proteins
Keywords	covid19
Language	English
Publishing date	2020-04-22
Publishing country	Germany
Document type	Journal Article
ZDB-ID	120933-4
ISSN	1432-1831 ; 0300-8584
ISSN (online)	1432-1831
ISSN	0300-8584
DOI	10.1007/s00430-020-00675-1
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Article ; Online: A Hepatitis C virus genotype 1b post-transplant isolate with high replication efficiency in cell culture and its adaptation to infectious virus production in vitro and in vivo.

Heuss, Christian / Rothhaar, Paul / Burm, Rani / Lee, Ji-Young / Ralfs, Philipp / Haselmann, Uta / Ströh, Luisa J / Colasanti, Ombretta / Tran, Cong Si / Schäfer, Noemi / Schnitzler, Paul / Merle, Uta / Bartenschlager, Ralf / Patel, Arvind H / Graw, Frederik / Krey, Thomas / Laketa, Vibor / Meuleman, Philip / Lohmann, Volker

PLoS pathogens

2022 Volume 18, Issue 6, Page(s) e1010472

Abstract: Hepatitis C virus (HCV) is highly diverse and grouped into eight genotypes (gts). Infectious cell culture models are limited to a few subtypes and isolates, hampering the development of prophylactic vaccines. A consensus gt1b genome (termed GLT1) was ... ...

Abstract	Hepatitis C virus (HCV) is highly diverse and grouped into eight genotypes (gts). Infectious cell culture models are limited to a few subtypes and isolates, hampering the development of prophylactic vaccines. A consensus gt1b genome (termed GLT1) was generated from an HCV infected liver-transplanted patient. GLT1 replicated to an outstanding efficiency in Huh7 cells upon SEC14L2 expression, by use of replication enhancing mutations or with a previously developed inhibitor-based regimen. RNA replication levels almost reached JFH-1, but full-length genomes failed to produce detectable amounts of infectious virus. Long-term passaging led to the adaptation of a genome carrying 21 mutations and concomitant production of high levels of transmissible infectivity (GLT1cc). During the adaptation, GLT1 spread in the culture even in absence of detectable amounts of free virus, likely due to cell-to-cell transmission, which appeared to substantially contribute to spreading of other isolates as well. Mechanistically, genome replication and particle production efficiency were enhanced by adaptation, while cell entry competence of HCV pseudoparticles was not affected. Furthermore, GLT1cc retained the ability to replicate in human liver chimeric mice, which was critically dependent on a mutation in domain 3 of nonstructural protein NS5A. Over the course of infection, only one mutation in the surface glycoprotein E2 consistently reverted to wildtype, facilitating assembly in cell culture but potentially affecting CD81 interaction in vivo. Overall, GLT1cc is an efficient gt1b infectious cell culture model, paving the road to a rationale-based establishment of new infectious HCV isolates and represents an important novel tool for the development of prophylactic HCV vaccines.
MeSH term(s)	Animals ; Cell Culture Techniques ; Genotype ; Hepacivirus ; Hepatitis C ; Humans ; Mice ; Mutation ; Viral Nonstructural Proteins/metabolism ; Virus Replication
Chemical Substances	Viral Nonstructural Proteins
Language	English
Publishing date	2022-06-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010472
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