LIVIVO - Search results -

Search results

Result 1 - 10 of total 54

Search options

Article: Anti-Immune Complex Antibodies are Elicited During Repeated Immunization with HIV Env Immunogens.

Brown, Sharidan / Antanasijevic, Aleksandar / Sewall, Leigh M / Garcia, Daniel Montiel / Brouwer, Philip J M / Sanders, Rogier W / Ward, Andrew B

bioRxiv : the preprint server for biology

2024

Abstract: Vaccination strategies against HIV-1 aim to elicit broadly neutralizing antibodies (bnAbs) using prime-boost regimens with HIV envelope (Env) immunogens. Early antibody responses to easily accessible epitopes on these antigens are directed to non- ... ...

Abstract	Vaccination strategies against HIV-1 aim to elicit broadly neutralizing antibodies (bnAbs) using prime-boost regimens with HIV envelope (Env) immunogens. Early antibody responses to easily accessible epitopes on these antigens are directed to non-neutralizing epitopes instead of bnAb epitopes. Autologous neutralizing antibody responses appear upon boosting once immunodominant epitopes are saturated. Here we report another type of antibody response that arises after repeated immunizations with HIV Env immunogens and present the structures of six anti-immune complexes discovered using polyclonal epitope mapping. The anti-immune complex antibodies target idiotopes composed of framework regions of antibodies bound to Env. This work sheds light on current vaccine development efforts for HIV, as well as for other pathogens, in which repeated exposure to antigen is required.
Language	English
Publishing date	2024-03-17
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.03.15.585257
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Presentation of HIV-1 envelope glycoprotein trimers on diverse nanoparticle platforms.

Brouwer, Philip J M / Sanders, Rogier W

Current opinion in HIV and AIDS

2019 Volume 14, Issue 4, Page(s) 302–308

Abstract: Purpose of review: We will discuss recent advances in the development of nanoparticle vaccines presenting HIV-1 envelope trimer vaccines and the immunological mechanisms by which they act.: Recent findings: The multivalent presentation of Env trimers ...

Abstract	Purpose of review: We will discuss recent advances in the development of nanoparticle vaccines presenting HIV-1 envelope trimer vaccines and the immunological mechanisms by which they act. Recent findings: The multivalent presentation of Env trimers on nanoparticles is a promising strategy to increase Env immunogenicity. Recent studies have shed light on how Env nanoparticles increase lymph node trafficking and germinal center formation by using the lectin-mediated complement pathway and enhancing the interaction with naïve B cells. Meanwhile, research on different nanoparticle platforms has resulted in improved designs, such as liposomes with improved stability, and the emergence of novel platforms such as protein nanoparticles that self-assemble in vitro. Immmunogenicity studies with these nanoparticles delineate the advantages and expose the limitations of the different nanoparticle platforms. Summary: It is becoming increasingly clear that HIV-1 vaccine research might benefit greatly from using nanoparticles presenting Env trimers, particularly during the priming stage of immunization. Among the different nanoparticles that are being pursued, in vitro-assembling nanoparticles allow for greater control of Env quality making them a promising nanoparticle platform.
MeSH term(s)	AIDS Vaccines/administration & dosage ; AIDS Vaccines/chemistry ; AIDS Vaccines/immunology ; Animals ; B-Lymphocytes/immunology ; HIV Infections/immunology ; HIV Infections/prevention & control ; HIV Infections/virology ; HIV-1/genetics ; HIV-1/immunology ; Humans ; Nanoparticles/administration & dosage ; Nanoparticles/chemistry ; Vaccination ; env Gene Products, Human Immunodeficiency Virus/chemistry ; env Gene Products, Human Immunodeficiency Virus/genetics ; env Gene Products, Human Immunodeficiency Virus/immunology
Chemical Substances	AIDS Vaccines ; env Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2019-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2502511-9
ISSN	1746-6318 ; 1746-630X
ISSN (online)	1746-6318
ISSN	1746-630X
DOI	10.1097/COH.0000000000000549
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6812: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses.

Brouwer, Philip J M / Perrett, Hailee R / Beaumont, Tim / Nijhuis, Haye / Kruijer, Sabine / Burger, Judith A / Lee, Wen-Hsin / Müller-Kraüter, Helena / Sanders, Rogier W / Strecker, Thomas / van Gils, Marit J / Ward, Andrew B

bioRxiv : the preprint server for biology

2023

Abstract: Lassa fever continues to be a major public health burden in endemic countries in West Africa, yet effective therapies or vaccines are lacking. The isolation of potent and protective neutralizing antibodies against the Lassa virus glycoprotein complex ( ... ...

Abstract	Lassa fever continues to be a major public health burden in endemic countries in West Africa, yet effective therapies or vaccines are lacking. The isolation of potent and protective neutralizing antibodies against the Lassa virus glycoprotein complex (GPC) justifies the development of vaccines that can elicit strong neutralizing antibody responses. However, Lassa vaccines candidates have generally been unsuccessful in doing so and the associated antibody responses to these vaccines remain poorly characterized. Here, we establish an electron-microscopy based epitope mapping pipeline that enables high-resolution structural characterization of polyclonal antibodies to GPC. By applying this method to rabbits vaccinated with a recombinant GPC vaccine and a GPC-derived virus-like particle, we reveal determinants of neutralization which involve epitopes of the GPC-C, GPC-A, and GP1-A competition clusters. Furthermore, by identifying previously undescribed immunogenic off-target epitopes, we expose challenges that recombinant GPC vaccines face. By enabling detailed polyclonal antibody characterization, our work ushers in a next generation of more rational Lassa vaccine design.
Language	English
Publishing date	2023-12-23
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.12.21.572918
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article: New Monoclonal Antibodies Specific for Different Epitopes of the Spike Protein of SARS-CoV-2 and Its Major Variants: Additional Tools for a More Specific COVID-19 Diagnosis.

Mariotti, Sabrina / Chiantore, Maria Vincenza / Teloni, Raffaela / Iacobino, Angelo / Capocefalo, Antonio / Michelini, Zuleika / Borghi, Martina / Baggieri, Melissa / Marchi, Antonella / Bucci, Paola / Gioacchini, Silvia / D'Amelio, Raffaele / Brouwer, Philip J M / Sandini, Silvia / Acchioni, Chiara / Sgarbanti, Marco / Di Virgilio, Antonio / Grasso, Felicia / Cara, Andrea /

Negri, Donatella / Magurano, Fabio / Di Bonito, Paola / Nisini, Roberto

Biomedicines

2023 Volume 11, Issue 2

Abstract: The emergence of the new pathogen SARS-CoV-2 determined a rapid need for monoclonal antibodies (mAbs) to detect the virus in biological fluids as a rapid tool to identify infected individuals to be treated or quarantined. The majority of commercially ... ...

Abstract	The emergence of the new pathogen SARS-CoV-2 determined a rapid need for monoclonal antibodies (mAbs) to detect the virus in biological fluids as a rapid tool to identify infected individuals to be treated or quarantined. The majority of commercially available antigenic tests for SARS-CoV-2 rely on the detection of N antigen in biologic fluid using anti-N antibodies, and their capacity to specifically identify subjects infected by SARS-CoV-2 is questionable due to several structural analogies among the N proteins of different coronaviruses. In order to produce new specific antibodies, BALB/c mice were immunized three times at 20-day intervals with a recombinant spike (S) protein. The procedure used was highly efficient, and 40 different specific mAbs were isolated, purified and characterized, with 13 ultimately being selected for their specificity and lack of cross reactivity with other human coronaviruses. The specific epitopes recognized by the selected mAbs were identified through a peptide library and/or by recombinant fragments of the S protein. In particular, the selected mAbs recognized different linear epitopes along the S1, excluding the receptor binding domain, and along the S2 subunits of the S protein of SARS-CoV-2 and its major variants of concern. We identified combinations of anti-S mAbs suitable for use in ELISA or rapid diagnostic tests, with the highest sensitivity and specificity coming from proof-of-concept tests using recombinant antigens, SARS-CoV-2 or biological fluids from infected individuals, that represent important additional tools for the diagnosis of COVID-19.
Language	English
Publishing date	2023-02-18
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720867-9
ISSN	2227-9059
ISSN	2227-9059
DOI	10.3390/biomedicines11020610
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies.

Perrett, Hailee R / Brouwer, Philip J M / Hurtado, Jonathan / Newby, Maddy L / Liu, Lin / Müller-Kräuter, Helena / Müller Aguirre, Sarah / Burger, Judith A / Bouhuijs, Joey H / Gibson, Grace / Messmer, Terrence / Schieffelin, John S / Antanasijevic, Aleksandar / Boons, Geert-Jan / Strecker, Thomas / Crispin, Max / Sanders, Rogier W / Briney, Bryan / Ward, Andrew B

Cell reports

2023 Volume 42, Issue 5, Page(s) 112524

Abstract: Lassa fever is an acute hemorrhagic fever caused by the zoonotic Lassa virus (LASV). The LASV glycoprotein complex (GPC) mediates viral entry and is the sole target for neutralizing antibodies. Immunogen design is complicated by the metastable nature of ... ...

Abstract	Lassa fever is an acute hemorrhagic fever caused by the zoonotic Lassa virus (LASV). The LASV glycoprotein complex (GPC) mediates viral entry and is the sole target for neutralizing antibodies. Immunogen design is complicated by the metastable nature of recombinant GPCs and the antigenic differences among phylogenetically distinct LASV lineages. Despite the sequence diversity of the GPC, structures of most lineages are lacking. We present the development and characterization of prefusion-stabilized, trimeric GPCs of LASV lineages II, V, and VII, revealing structural conservation despite sequence diversity. High-resolution structures and biophysical characterization of the GPC in complex with GP1-A-specific antibodies suggest their neutralization mechanisms. Finally, we present the isolation and characterization of a trimer-preferring neutralizing antibody belonging to the GPC-B competition group with an epitope that spans adjacent protomers and includes the fusion peptide. Our work provides molecular detail information on LASV antigenic diversity and will guide efforts to design pan-LASV vaccines.
MeSH term(s)	Humans ; Lassa virus ; Antibodies, Neutralizing ; Lassa Fever/prevention & control ; Glycoproteins ; Antigens, Viral
Chemical Substances	Antibodies, Neutralizing ; Glycoproteins ; Antigens, Viral
Language	English
Publishing date	2023-05-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112524
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: SARS-CoV-2 infection activates dendritic cells via cytosolic receptors rather than extracellular TLRs.

van der Donk, Lieve E H / Eder, Julia / van Hamme, John L / Brouwer, Philip J M / Brinkkemper, Mitch / van Nuenen, Ad C / van Gils, Marit J / Sanders, Rogier W / Kootstra, Neeltje A / Bermejo-Jambrina, Marta / Geijtenbeek, Teunis B H

European journal of immunology

2022 Volume 52, Issue 4, Page(s) 646–655

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes coronavirus disease 2019 (COVID-19), an infectious disease characterized by strong induction of inflammatory cytokines, progressive lung inflammation, and potentially multiorgan ... ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes coronavirus disease 2019 (COVID-19), an infectious disease characterized by strong induction of inflammatory cytokines, progressive lung inflammation, and potentially multiorgan dysfunction. It remains unclear how SARS-CoV-2 infection leads to immune activation. The Spike (S) protein of SARS-CoV-2 has been suggested to trigger TLR4 and thereby activate immunity. Here, we have investigated the role of TLR4 in SARS-CoV-2 infection and immunity. Neither exposure of isolated S protein, SARS-CoV-2 pseudovirus nor primary SARS-CoV-2 isolate induced TLR4 activation in a TLR4-expressing cell line. Human monocyte-derived DCs express TLR4 but not angiotensin converting enzyme 2 (ACE2), and DCs were not infected by SARS-CoV-2. Notably, neither S protein nor SARS-CoV-2 induced DC maturation or cytokines, indicating that both S protein and SARS-CoV-2 virus particles do not trigger extracellular TLRs including TLR4. Ectopic expression of ACE2 in DCs led to efficient infection by SARS-CoV-2 and, strikingly, efficient type I IFN and cytokine responses. These data strongly suggest that not extracellular TLRs but intracellular viral sensors are key players in sensing SARS-CoV-2. These data imply that SARS-CoV-2 escapes direct sensing by TLRs, which might underlie the lack of efficient immunity to SARS-CoV-2 early during infection.
MeSH term(s)	COVID-19/immunology ; Cell Line ; Dendritic Cells/immunology ; Humans ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/immunology ; Toll-Like Receptor 4/immunology
Chemical Substances	Spike Glycoprotein, Coronavirus ; TLR4 protein, human ; Toll-Like Receptor 4 ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-02-16
Publishing country	Germany
Document type	Journal Article
ZDB-ID	120108-6
ISSN	1521-4141 ; 0014-2980
ISSN (online)	1521-4141
ISSN	0014-2980
DOI	10.1002/eji.202149656
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 489: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 85: Show issues

Order via subito

Details ▾

Article: Probing Affinity, Avidity, Anticooperativity, and Competition in Antibody and Receptor Binding to the SARS-CoV-2 Spike by Single Particle Mass Analyses.

Yin, Victor / Lai, Szu-Hsueh / Caniels, Tom G / Brouwer, Philip J M / Brinkkemper, Mitch / Aldon, Yoann / Liu, Hejun / Yuan, Meng / Wilson, Ian A / Sanders, Rogier W / van Gils, Marit J / Heck, Albert J R

ACS central science

2021 Volume 7, Issue 11, Page(s) 1863–1873

Abstract: Determining how antibodies interact with the spike (S) protein of the SARS-CoV-2 virus is critical for combating COVID-19. Structural studies typically employ simplified, truncated constructs that may not fully recapitulate the behavior of the original ... ...

Abstract	Determining how antibodies interact with the spike (S) protein of the SARS-CoV-2 virus is critical for combating COVID-19. Structural studies typically employ simplified, truncated constructs that may not fully recapitulate the behavior of the original complexes. Here, we combine two single particle mass analysis techniques (mass photometry and charge-detection mass spectrometry) to enable the measurement of full IgG binding to the trimeric SARS-CoV-2 S ectodomain. Our experiments reveal that antibodies targeting the S-trimer typically prefer stoichiometries lower than the symmetry-predicted 3:1 binding. We determine that this behavior arises from the interplay of steric clashes and avidity effects that are not reflected in common antibody constructs (i.e., Fabs). Surprisingly, these substoichiometric complexes are fully effective at blocking ACE2 binding despite containing free receptor binding sites. Our results highlight the importance of studying antibody/antigen interactions using complete, multimeric constructs and showcase the utility of single particle mass analyses in unraveling these complex interactions.
Language	English
Publishing date	2021-11-04
Publishing country	United States
Document type	Journal Article
ISSN	2374-7943
ISSN	2374-7943
DOI	10.1021/acscentsci.1c00804
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Diagnostic performance of two serological assays for the detection of SARS-CoV-2 specific antibodies: surveillance after vaccination.

Fresco-Taboada, Alba / García-Durán, Marga / Aira, Cristina / López, Lissett / Sastre, Patricia / van der Hoek, Lia / van Gils, Marit J / Brouwer, Philip J M / Sanders, Rogier W / Holzer, Barbara / Zimpernikc, Irene / López-Collazo, Eduardo / Muñoz, Patricia / Rueda, Paloma / Vela, Carmen

Diagnostic microbiology and infectious disease

2022 Volume 102, Issue 4, Page(s) 115650

Abstract: Massive vaccination programs are being carried out to limit the SARS-CoV-2 pandemic that started in December 2019. Serological tests are of major importance as an indicator of circulation of the virus and to assess how vaccine-induced immunity progresses. ...

Abstract	Massive vaccination programs are being carried out to limit the SARS-CoV-2 pandemic that started in December 2019. Serological tests are of major importance as an indicator of circulation of the virus and to assess how vaccine-induced immunity progresses. An Enzyme-Linked Immunosorbent Assay (ELISA) and a Lateral Flow Assay (LFA) have been developed based on the SARS-CoV-2 recombinant Receptor Binding Domain (RBD) and the combination of Spike and Nucleoprotein, respectively. The validation with 1272 serum samples by comparison with INgezim COVID 19 DR showed good diagnostic performance (sensitivity: 93.2%-97.2%; specificity: 98.3%-99.3%) for detection of previous contact with SARS-CoV-2. Moreover, according to our results, these assays can help in the serosurveillance during and after vaccination, by detecting the humoral immune response as soon as 15 days postvaccination and identifying low-respondents. Hence, these tests could play a key role in the progression to a COVID-19 free world, helping to adjust future vaccination protocols.
MeSH term(s)	Antibodies, Viral ; COVID-19/diagnosis ; COVID-19/prevention & control ; Humans ; SARS-CoV-2 ; Sensitivity and Specificity ; Spike Glycoprotein, Coronavirus ; Vaccination
Chemical Substances	Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-01-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	604920-5
ISSN	1879-0070 ; 0732-8893
ISSN (online)	1879-0070
ISSN	0732-8893
DOI	10.1016/j.diagmicrobio.2022.115650
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1845: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A Lassa virus mRNA vaccine confers protection but does not require neutralizing antibody in a guinea pig model of infection.

Ronk, Adam J / Lloyd, Nicole M / Zhang, Min / Atyeo, Caroline / Perrett, Hailee R / Mire, Chad E / Hastie, Kathryn M / Sanders, Rogier W / Brouwer, Philip J M / Saphire, Erica Olmann / Ward, Andrew B / Ksiazek, Thomas G / Alvarez Moreno, Juan Carlos / Thaker, Harshwardhan M / Alter, Galit / Himansu, Sunny / Carfi, Andrea / Bukreyev, Alexander

Nature communications

2023 Volume 14, Issue 1, Page(s) 5603

Abstract: Lassa virus is a member of the Arenaviridae family, which causes human infections ranging from asymptomatic to severe hemorrhagic disease with a high case fatality rate. We have designed and generated lipid nanoparticle encapsulated, modified mRNA ... ...

Abstract	Lassa virus is a member of the Arenaviridae family, which causes human infections ranging from asymptomatic to severe hemorrhagic disease with a high case fatality rate. We have designed and generated lipid nanoparticle encapsulated, modified mRNA vaccines that encode for the wild-type Lassa virus strain Josiah glycoprotein complex or the prefusion stabilized conformation of the Lassa virus glycoprotein complex. Hartley guinea pigs were vaccinated with two 10 µg doses, 28 days apart, of either construct. Vaccination induced strong binding antibody responses, specific to the prefusion conformation of glycoprotein complex, which were significantly higher in the prefusion stabilized glycoprotein complex construct group and displayed strong Fc-mediated effects. However, Lassa virus-neutralizing antibody activity was detected in some but not all animals. Following the challenge with a lethal dose of the Lassa virus, all vaccinated animals were protected from death and severe disease. Although the definitive mechanism of protection is still unknown, and assessment of the cell-mediated immune response was not investigated in this study, these data demonstrate the promise of mRNA as a vaccine platform against the Lassa virus and that protection against Lassa virus can be achieved in the absence of virus-neutralizing antibodies.
MeSH term(s)	Humans ; Guinea Pigs ; Animals ; Lassa virus/genetics ; Antibodies, Neutralizing ; Arenaviridae ; mRNA Vaccines ; Glycoproteins
Chemical Substances	Antibodies, Neutralizing ; mRNA Vaccines ; Glycoproteins
Language	English
Publishing date	2023-09-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-41376-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Author Correction: Interplay of diverse adjuvants and nanoparticle presentation of native-like HIV-1 envelope trimers.

Sliepen, Kwinten / Schermer, Edith / Bontjer, Ilja / Burger, Judith A / Lévai, Réka Felfödiné / Mundsperger, Philipp / Brouwer, Philip J M / Tolazzi, Monica / Farsang, Attila / Katinger, Dietmar / Moore, John P / Scarlatti, Gabriella / Shattock, Robin J / Sattentau, Quentin J / Sanders, Rogier W

NPJ vaccines

2021 Volume 6, Issue 1, Page(s) 134

Language	English
Publishing date	2021-11-02
Publishing country	England
Document type	Published Erratum
ISSN	2059-0105
ISSN (online)	2059-0105
DOI	10.1038/s41541-021-00398-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED