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Article ; Online: Can we recommend varicocele surgery for men with hypogonadism?

Marquardt, Nilson Filho / Da Ros, Carlos Teodósio

International braz j urol : official journal of the Brazilian Society of Urology

2023 Volume 49, Issue 5, Page(s) 637–643

MeSH term(s)	Male ; Humans ; Varicocele/complications ; Varicocele/surgery ; Hypogonadism/surgery ; Testosterone ; Infertility, Male
Chemical Substances	Testosterone (3XMK78S47O)
Language	English
Publishing date	2023-08-25
Publishing country	Brazil
Document type	Editorial
ZDB-ID	2206649-4
ISSN	1677-6119 ; 1677-5538
ISSN (online)	1677-6119
ISSN	1677-5538
DOI	10.1590/S1677-5538.IBJU.2023.0190
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Article ; Online: A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells.

Bircher, Cornelia / Bieri, Jan / Assaraf, Ruben / Leisi, Remo / Ros, Carlos

Viruses

2022 Volume 14, Issue 2

Abstract: Parvovirus B19 (B19V) is a human pathogen with a marked tropism for erythroid progenitor cells (EPCs). The N-terminal of the VP1 unique region (VP1u) contains a receptor-binding domain (RBD), which mediates virus uptake through interaction with an as-yet- ...

Abstract	Parvovirus B19 (B19V) is a human pathogen with a marked tropism for erythroid progenitor cells (EPCs). The N-terminal of the VP1 unique region (VP1u) contains a receptor-binding domain (RBD), which mediates virus uptake through interaction with an as-yet-unknown receptor (VP1uR). Considering the central role of VP1uR in the virus tropism, we sought to investigate its expression profile in multiple cell types. To this end, we established a PP7 bacteriophage-VP1u bioconjugate, sharing the size and VP1u composition of native B19V capsids. The suitability of the PP7-VP1u construct as a specific and sensitive VP1uR expression marker was validated in competition assays with B19V and recombinant VP1u. VP1uR expression was exclusively detected in erythroid cells and cells reprogrammed towards the erythroid lineage. Sequence alignment and in silico protein structure prediction of the N-terminal of VP1u (N-VP1u) from B19V and other primate erythroparvoviruses (simian, rhesus, and pig-tailed) revealed a similar structure characterized by a fold of three or four α-helices. Functional studies with simian parvovirus confirmed the presence of a conserved RBD in the N-VP1u, mediating virus internalization into human erythroid cells. In summary, this study confirms the exclusive association of VP1uR expression with cells of the erythroid lineage. The presence of an analogous RBD in the VP1u from non-human primate erythroparvoviruses emphasizes their parallel evolutionary trait and zoonotic potential.
MeSH term(s)	Animals ; Capsid Proteins/physiology ; Cell Line ; Erythroid Cells/metabolism ; Humans ; Parvovirus B19, Human/physiology ; Primates ; Protein Binding ; Receptors, Virus ; Viral Tropism ; Virus Internalization
Chemical Substances	Capsid Proteins ; Receptors, Virus
Language	English
Publishing date	2022-02-17
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/v14020420
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Article ; Online: Globoside Is Dispensable for Parvovirus B19 Entry but Essential at a Postentry Step for Productive Infection.

Bieri, Jan / Ros, Carlos

Journal of virology

2019 Volume 93, Issue 20

Abstract: Globoside (Gb4) is considered the primary receptor of parvovirus B19 (B19V); however, its expression does not correlate well with the attachment and restricted tropism of the virus. The N terminus of VP1 (VP1u) of B19V interacts with an as-yet-unknown ... ...

Abstract	Globoside (Gb4) is considered the primary receptor of parvovirus B19 (B19V); however, its expression does not correlate well with the attachment and restricted tropism of the virus. The N terminus of VP1 (VP1u) of B19V interacts with an as-yet-unknown receptor required for virus internalization. In contrast to Gb4, the VP1u cognate receptor is expressed exclusively in cells that B19V can internalize. With the aim of clarifying the role of Gb4 as a B19V receptor, we knocked out the gene B3GalNT1 coding for the enzyme globoside synthase in UT7/Epo cells. Consequently, B3GalNT1 transcripts and Gb4 became undetectable in the knockout (KO) cells without affecting cell viability and proliferation. Unexpectedly, virus attachment, internalization, and nuclear targeting were not disturbed in the KO cells. However, NS1 transcription failed, and consequently, genome replication and capsid protein expression were abrogated. The block could be circumvented by transfection with a B19V infectious clone, indicating that Gb4 is not required after the generation of viral double-stranded DNA with resolved inverted terminal repeats. While in wild-type (WT) cells, occupation of the VP1u cognate receptor with recombinant VP1u disturbed virus binding and blocked the infection, antibodies against Gb4 had no significant effect. In a mixed population of WT and KO cells, B19V selectively infected WT cells. This study demonstrates that Gb4 does not have the expected receptor function, as it is dispensable for virus entry; however, it is essential for productive infection, explaining the resistance of the rare individuals lacking Gb4 to B19V infection.
MeSH term(s)	Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Cell Line ; Cells, Cultured ; Erythema Infectiosum/metabolism ; Erythema Infectiosum/virology ; Gene Knockdown Techniques ; Globosides/metabolism ; Host-Pathogen Interactions ; Humans ; Parvovirus B19, Human/physiology ; Protein Binding ; Receptors, Virus/metabolism ; Viral Nonstructural Proteins/metabolism ; Virus Internalization ; Virus Replication
Chemical Substances	Capsid Proteins ; Globosides ; NS1 protein, parvovirus ; Receptors, Virus ; Viral Nonstructural Proteins
Language	English
Publishing date	2019-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00972-19
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Globoside and the mucosal pH mediate parvovirus B19 entry through the epithelial barrier.

Suter, Corinne / Colakovic, Minela / Bieri, Jan / Gultom, Mitra / Dijkman, Ronald / Ros, Carlos

PLoS pathogens

2023 Volume 19, Issue 5, Page(s) e1011402

Abstract: Parvovirus B19 (B19V) is transmitted primarily via the respiratory route, however, the mechanism involved remains unknown. B19V targets a restricted receptor expressed in erythroid progenitor cells in the bone marrow. However, B19V shifts the receptor ... ...

Abstract	Parvovirus B19 (B19V) is transmitted primarily via the respiratory route, however, the mechanism involved remains unknown. B19V targets a restricted receptor expressed in erythroid progenitor cells in the bone marrow. However, B19V shifts the receptor under acidic conditions and targets the widely expressed globoside. The pH-dependent interaction with globoside may allow virus entry through the naturally acidic nasal mucosa. To test this hypothesis, MDCK II cells and well-differentiated human airway epithelial cell (hAEC) cultures were grown on porous membranes and used as models to study the interaction of B19V with the epithelial barrier. Globoside expression was detected in polarized MDCK II cells and the ciliated cell population of well-differentiated hAEC cultures. Under the acidic conditions of the nasal mucosa, virus attachment and transcytosis occurred without productive infection. Neither virus attachment nor transcytosis was observed under neutral pH conditions or in globoside knockout cells, demonstrating the concerted role of globoside and acidic pH in the transcellular transport of B19V. Globoside-dependent virus uptake involved VP2 and occurred by a clathrin-independent pathway that is cholesterol and dynamin-dependent. This study provides mechanistic insight into the transmission of B19V through the respiratory route and reveals novel vulnerability factors of the epithelial barrier to viruses.
MeSH term(s)	Animals ; Dogs ; Humans ; Parvovirus B19, Human ; Globosides/metabolism ; Cell Line ; Mucous Membrane/metabolism ; Madin Darby Canine Kidney Cells
Chemical Substances	Globosides
Language	English
Publishing date	2023-05-23
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.1011402
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Article ; Online: Human parvovirus B19 interacts with globoside under acidic conditions as an essential step in endocytic trafficking.

Bieri, Jan / Leisi, Remo / Bircher, Cornelia / Ros, Carlos

PLoS pathogens

2021 Volume 17, Issue 4, Page(s) e1009434

Abstract: The glycosphingolipid (GSL) globoside (Gb4) is essential for parvovirus B19 (B19V) infection. Historically considered the cellular receptor of B19V, the role of Gb4 and its interaction with B19V are controversial. In this study, we applied artificial ... ...

Abstract	The glycosphingolipid (GSL) globoside (Gb4) is essential for parvovirus B19 (B19V) infection. Historically considered the cellular receptor of B19V, the role of Gb4 and its interaction with B19V are controversial. In this study, we applied artificial viral particles, genetically modified cells, and specific competitors to address the interplay between the virus and the GSL. Our findings demonstrate that Gb4 is not involved in the binding or internalization process of the virus into permissive erythroid cells, a function that corresponds to the VP1u cognate receptor. However, Gb4 is essential at a post-internalization step before the delivery of the single-stranded viral DNA into the nucleus. In susceptible erythroid Gb4 knockout cells, incoming viruses were arrested in the endosomal compartment, showing no cytoplasmic spreading of capsids as observed in Gb4-expressing cells. Hemagglutination and binding assays revealed that pH acts as a switch to modulate the affinity between the virus and the GSL. Capsids interact with Gb4 exclusively under acidic conditions and dissociate at neutral pH. Inducing a specific Gb4-mediated attachment to permissive erythroid cells by acidification of the extracellular environment led to a non-infectious uptake of the virus, indicating that low pH-mediated binding to the GSL initiates active membrane processes resulting in vesicle formation. In summary, this study provides mechanistic insight into the interaction of B19V with Gb4. The strict pH-dependent binding to the ubiquitously expressed GSL prevents the redirection of the virus to nonpermissive tissues while promoting the interaction in acidic intracellular compartments as an essential step in infectious endocytic trafficking.
MeSH term(s)	Capsid/metabolism ; Capsid Proteins/drug effects ; Capsid Proteins/metabolism ; Endocytosis/immunology ; Endocytosis/physiology ; Globosides/metabolism ; Glycosphingolipids/metabolism ; Humans ; Parvovirus B19, Human/genetics ; Parvovirus B19, Human/pathogenicity ; Receptors, Virus/drug effects ; Receptors, Virus/metabolism ; Virion/drug effects ; Virion/metabolism ; Virus Internalization/drug effects
Chemical Substances	Capsid Proteins ; Globosides ; Glycosphingolipids ; Receptors, Virus
Language	English
Publishing date	2021-04-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1009434
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells

Bircher, Cornelia / Bieri, Jan / Assaraf, Ruben / Leisi, Remo / Ros, Carlos

Viruses. 2022 Feb. 17, v. 14, no. 2

2022

Abstract	Parvovirus B19 (B19V) is a human pathogen with a marked tropism for erythroid progenitor cells (EPCs). The N-terminal of the VP1 unique region (VP1u) contains a receptor-binding domain (RBD), which mediates virus uptake through interaction with an as-yet-unknown receptor (VP1uR). Considering the central role of VP1uR in the virus tropism, we sought to investigate its expression profile in multiple cell types. To this end, we established a PP7 bacteriophage-VP1u bioconjugate, sharing the size and VP1u composition of native B19V capsids. The suitability of the PP7-VP1u construct as a specific and sensitive VP1uR expression marker was validated in competition assays with B19V and recombinant VP1u. VP1uR expression was exclusively detected in erythroid cells and cells reprogrammed towards the erythroid lineage. Sequence alignment and in silico protein structure prediction of the N-terminal of VP1u (N-VP1u) from B19V and other primate erythroparvoviruses (simian, rhesus, and pig-tailed) revealed a similar structure characterized by a fold of three or four α-helices. Functional studies with simian parvovirus confirmed the presence of a conserved RBD in the N-VP1u, mediating virus internalization into human erythroid cells. In summary, this study confirms the exclusive association of VP1uR expression with cells of the erythroid lineage. The presence of an analogous RBD in the VP1u from non-human primate erythroparvoviruses emphasizes their parallel evolutionary trait and zoonotic potential.
Keywords	Protoparvovirus ; Simian parvovirus ; animal pathogens ; capsid ; computer simulation ; humans ; prediction ; protein structure ; sequence alignment ; viruses ; zoonoses
Language	English
Dates of publication	2022-0217
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v14020420
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The VP1u of Human Parvovirus B19: A Multifunctional Capsid Protein with Biotechnological Applications.

Ros, Carlos / Bieri, Jan / Leisi, Remo

Viruses

2020 Volume 12, Issue 12

Abstract: The viral protein 1 unique region (VP1u) of human parvovirus B19 (B19V) is a multifunctional capsid protein with essential roles in virus tropism, uptake, and subcellular trafficking. These functions reside on hidden protein domains, which become ... ...

Abstract	The viral protein 1 unique region (VP1u) of human parvovirus B19 (B19V) is a multifunctional capsid protein with essential roles in virus tropism, uptake, and subcellular trafficking. These functions reside on hidden protein domains, which become accessible upon interaction with cell membrane receptors. A receptor-binding domain (RBD) in VP1u is responsible for the specific targeting and uptake of the virus exclusively into cells of the erythroid lineage in the bone marrow. A phospholipase A
MeSH term(s)	Binding Sites ; Biotechnology ; Capsid Proteins/chemistry ; Capsid Proteins/immunology ; Capsid Proteins/physiology ; Immunodominant Epitopes ; Nuclear Localization Signals ; Parvovirus B19, Human/physiology ; Phospholipases A2/chemistry ; Receptors, Virus ; Viral Tropism ; Virion/physiology
Chemical Substances	Capsid Proteins ; Immunodominant Epitopes ; Nuclear Localization Signals ; Receptors, Virus ; capsid protein VP1, parvovirus B19 ; Phospholipases A2 (EC 3.1.1.4)
Language	English
Publishing date	2020-12-18
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v12121463
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Editorial Comment: Effect of smoking cessation on sexu-al function in men aged 30 to 60 years.

Da Ros, Carlos Teodósio / Facio, Fernando Nestor

International braz j urol : official journal of the Brazilian Society of Urology

2020 Volume 46, Issue 4, Page(s) 649–650

MeSH term(s)	Adult ; Humans ; Male ; Middle Aged ; Risk Factors ; Smoking ; Smoking Cessation
Language	English
Publishing date	2020-05-05
Publishing country	Brazil
Document type	Editorial ; Comment
ZDB-ID	2206649-4
ISSN	1677-6119 ; 1677-5538
ISSN (online)	1677-6119
ISSN	1677-5538
DOI	10.1590/S1677-5538.IBJU.2019.0541.1
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Article ; Online: The role of clomiphene citrate in late onset male hypogonadism.

Da Ros, Carlos Teodósio / Da Ros, Lucas Uglione / Da Ros, João Pedro Uglione

International braz j urol : official journal of the Brazilian Society of Urology

2022 Volume 48, Issue 5, Page(s) 850–856

MeSH term(s)	Clomiphene/adverse effects ; Humans ; Hypogonadism/drug therapy ; Male ; Testosterone
Chemical Substances	Clomiphene (1HRS458QU2) ; Testosterone (3XMK78S47O)
Language	English
Publishing date	2022-02-12
Publishing country	Brazil
Document type	Editorial
ZDB-ID	2206649-4
ISSN	1677-6119 ; 1677-5538
ISSN (online)	1677-6119
ISSN	1677-5538
DOI	10.1590/S1677-5538.IBJU.2021.0724
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Visualizing protein fouling and its impact on parvovirus retention within distinct filter membrane morphologies

Leisi, Remo / Rostami, Iman / Laughhunn, Andrew / Bieri, Jan / Roth, Nathan J. / Widmer, Eleonora / Ros, Carlos

Journal of membrane science. 2022 Oct. 05, v. 659

2022

Abstract: Virus filtration is considered an effective and robust method to remove viral contaminants that may enter the manufacturing process of biotherapeutics. However, insights into the retention mechanism of viruses under the influence of different operating ... ...

Abstract	Virus filtration is considered an effective and robust method to remove viral contaminants that may enter the manufacturing process of biotherapeutics. However, insights into the retention mechanism of viruses under the influence of different operating conditions have been limited so far. In this work, we visualize the impact of filter fouling and flow decay on the retention of fluorescently labeled minute virus of mice (MVM) in asymmetric Planova 20N and nearly homogeneous Pegasus SV4 filter membranes. Filtration of feedstreams containing polyclonal human immunoglobulin G (IgG) revealed a complex interplay of different fouling mechanisms depending on high- or low-fouling solution properties, and characteristic for the distinct filter types. The asymmetric filter morphology – which allowed gradual foulant deposition across membrane zones with different pore sizes – provided a larger capacity for capture of fouling particulates as well as robust virus retention under challenging feedstream conditions. Taken together, our results demonstrate that different filtration conditions can lead to a combination of various, even opposing effects on virus retention depending on the membrane structure and pore size characteristics. The phenomena visualized in this work contribute to a better understanding of the underlying molecular mechanisms and provide cues for specific optimization of virus filtration processes.
Keywords	filtration ; humans ; immunoglobulin G ; particulates ; porosity ; viral contamination ; viruses
Language	English
Dates of publication	2022-1005
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	194516-6
ISSN	0376-7388
ISSN	0376-7388
DOI	10.1016/j.memsci.2022.120791
Database	NAL-Catalogue (AGRICOLA)

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