LIVIVO - Search results -

Search results

Result 1 - 10 of total 47

Search options

Article ; Online: Antigenic evolution of SARS coronavirus 2.

Mykytyn, Anna Z / Fouchier, Ron Am / Haagmans, Bart L

2023 Volume 62, Page(s) 101349

Abstract: SARS coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19, emerged in China in December 2019. Vaccines developed were very effective initially, however, the virus has shown remarkable evolution with multiple variants spreading globally over the ... ...

Abstract	SARS coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19, emerged in China in December 2019. Vaccines developed were very effective initially, however, the virus has shown remarkable evolution with multiple variants spreading globally over the last three years. Nowadays, newly emerging Omicron lineages are gaining substitutions at a fast rate, resulting in escape from neutralization by antibodies that target the Spike protein. Tools to map the impact of substitutions on the further antigenic evolution of SARS-CoV-2, such as antigenic cartography, may be helpful to update SARS-CoV-2 vaccines. In this review, we focus on the antigenic evolution of SARS-CoV-2, highlighting the impact of Spike protein substitutions individually and in combination on immune escape.
MeSH term(s)	Humans ; SARS-CoV-2/genetics ; COVID-19 ; COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus/genetics ; Antibodies
Chemical Substances	COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus ; Antibodies ; spike protein, SARS-CoV-2
Language	English
Publishing date	2023-08-28
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2611378-8
ISSN	1879-6265 ; 1879-6257
ISSN (online)	1879-6265
ISSN	1879-6257
DOI	10.1016/j.coviro.2023.101349
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

Article ; Online: Human metapneumovirus infection of organoid-derived human bronchial epithelium represents cell tropism and cytopathology as observed in

Ribó-Molina, Pau / van Nieuwkoop, Stefan / Mykytyn, Anna Z / van Run, Peter / Lamers, Mart M / Haagmans, Bart L / Fouchier, Ron A M / van den Hoogen, Bernadette G

mSphere

2024 Volume 9, Issue 2, Page(s) e0074323

Abstract: Human metapneumovirus (HMPV), a member of the : Importance: Human metapneumovirus (HMPV) is one of the leading causative agents of respiratory disease in humans, with no treatment or vaccine available yet. The use of primary epithelial cultures that ... ...

Abstract	Human metapneumovirus (HMPV), a member of the Importance: Human metapneumovirus (HMPV) is one of the leading causative agents of respiratory disease in humans, with no treatment or vaccine available yet. The use of primary epithelial cultures that recapitulate the tissue morphology and biochemistry of the human airways could aid in defining more relevant targets to prevent HMPV infection. For this purpose, this study established the first primary organoid-derived bronchial culture model suitable for a broad range of HMPV isolates. These bronchial cultures were assessed for HMPV replication, cellular tropism, cytopathology, and innate immune responses, where the observations were linked to previous
MeSH term(s)	Humans ; Animals ; Metapneumovirus/physiology ; Cytology ; Virus Replication ; Paramyxoviridae Infections/pathology ; Epithelium ; Macaca ; Tropism
Language	English
Publishing date	2024-01-24
Publishing country	United States
Document type	Journal Article
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/msphere.00743-23
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: Glycosylated extracellular mucin domains protect against SARS-CoV-2 infection at the respiratory surface.

Chatterjee, Maitrayee / Huang, Liane Z X / Mykytyn, Anna Z / Wang, Chunyan / Lamers, Mart M / Westendorp, Bart / Wubbolts, Richard W / van Putten, Jos P M / Bosch, Berend-Jan / Haagmans, Bart L / Strijbis, Karin

PLoS pathogens

2023 Volume 19, Issue 8, Page(s) e1011571

Abstract: Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by ... ...

Abstract	Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by mucociliary clearance. Transmembrane mucins MUC1, MUC4, and MUC16 can restrict microbial invasion at the apical surface of the epithelium. In this study, we determined the impact of host mucins and mucin glycans on epithelial entry of SARS-CoV-2. Human lung epithelial Calu-3 cells express the SARS-CoV-2 entry receptor ACE2 and high levels of glycosylated MUC1, but not MUC4 and MUC16, on their cell surface. The O-glycan-specific mucinase StcE specifically removed the glycosylated part of the MUC1 extracellular domain while leaving the underlying SEA domain and cytoplasmic tail intact. StcE treatment of Calu-3 cells significantly enhanced infection with SARS-CoV-2 pseudovirus and authentic virus, while removal of terminal mucin glycans sialic acid and fucose from the epithelial surface did not impact viral entry. In Calu-3 cells, the transmembrane mucin MUC1 and ACE2 are located to the apical surface in close proximity and StcE treatment results in enhanced binding of purified spike protein. Both MUC1 and MUC16 are expressed on the surface of human organoid-derived air-liquid interface (ALI) differentiated airway cultures and StcE treatment led to mucin removal and increased levels of SARS-CoV-2 replication. In these cultures, MUC1 was highly expressed in non-ciliated cells while MUC16 was enriched in goblet cells. In conclusion, the glycosylated extracellular domains of different transmembrane mucins might have similar protective functions in different respiratory cell types by restricting SARS-CoV-2 binding and entry.
MeSH term(s)	Humans ; Mucins/metabolism ; Angiotensin-Converting Enzyme 2 ; COVID-19 ; SARS-CoV-2/metabolism ; CA-125 Antigen/metabolism ; Lung/metabolism ; Polysaccharides
Chemical Substances	Mucins ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; CA-125 Antigen ; Polysaccharides
Language	English
Publishing date	2023-08-10
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.1011571
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: SARS-CoV-2 Omicron entry is type II transmembrane serine protease-mediated in human airway and intestinal organoid models.

Mykytyn, Anna Z / Breugem, Tim I / Geurts, Maarten H / Beumer, Joep / Schipper, Debby / van Acker, Romy / van den Doel, Petra B / van Royen, Martin E / Zhang, Jingshu / Clevers, Hans / Haagmans, Bart L / Lamers, Mart M

Journal of virology

2023 Volume 97, Issue 8, Page(s) e0085123

Abstract: SARS-CoV-2 can enter cells after its spike protein is cleaved by either type II transmembrane serine proteases (TTSPs), like TMPRSS2, or cathepsins. It is now widely accepted that the Omicron variant uses TMPRSS2 less efficiently and instead enters cells ...

Abstract	SARS-CoV-2 can enter cells after its spike protein is cleaved by either type II transmembrane serine proteases (TTSPs), like TMPRSS2, or cathepsins. It is now widely accepted that the Omicron variant uses TMPRSS2 less efficiently and instead enters cells via cathepsins, but these findings have yet to be verified in more relevant cell models. Although we could confirm efficient cathepsin-mediated entry for Omicron in a monkey kidney cell line, experiments with protease inhibitors showed that Omicron (BA.1 and XBB1.5) did not use cathepsins for entry into human airway organoids and instead utilized TTSPs. Likewise, CRISPR-edited intestinal organoids showed that entry of Omicron BA.1 relied on the expression of the serine protease TMPRSS2 but not cathepsin L or B. Together, these data force us to rethink the concept that Omicron has adapted to cathepsin-mediated entry and indicate that TTSP inhibitors should not be dismissed as prophylactic or therapeutic antiviral strategy against SARS-CoV-2. IMPORTANCE Coronavirus entry relies on host proteases that activate the viral fusion protein, spike. These proteases determine the viral entry route, tropism, host range, and can be attractive drug targets. Whereas earlier studies using cell lines suggested that the Omicron variant of SARS-CoV-2 has changed its protease usage, from cell surface type II transmembrane serine proteases (TTSPs) to endosomal cathepsins, we report that this is not the case in human airway and intestinal organoid models, suggesting that host TTSP inhibition is still a viable prophylactic or therapeutic antiviral strategy against current SARS-CoV-2 variants and highlighting the importance of relevant human
MeSH term(s)	Humans ; Antiviral Agents ; COVID-19/virology ; SARS-CoV-2/physiology ; Serine Proteases/metabolism ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Virus Internalization
Chemical Substances	Antiviral Agents ; Serine Proteases (EC 3.4.-) ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; TMPRSS2 protein, human (EC 3.4.21.-)
Language	English
Publishing date	2023-08-09
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.00851-23
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: 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: Antigenic mapping of emerging SARS-CoV-2 omicron variants BM.1.1.1, BQ.1.1, and XBB.1.

Mykytyn, Anna Z / Rosu, Miruna E / Kok, Adinda / Rissmann, Melanie / van Amerongen, Geert / Geurtsvankessel, Corine / de Vries, Rory D / Munnink, Bas B Oude / Smith, Derek J / Koopmans, Marion P G / Lamers, Mart M / Fouchier, Ron A M / Haagmans, Bart L

The Lancet. Microbe

2023 Volume 4, Issue 5, Page(s) e294–e295

MeSH term(s)	Humans ; COVID-19 ; SARS-CoV-2/genetics
Language	English
Publishing date	2023-01-16
Publishing country	England
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2666-5247
ISSN (online)	2666-5247
DOI	10.1016/S2666-5247(22)00384-6
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: Extended Viral Shedding of MERS-CoV Clade B Virus in Llamas Compared with African Clade C Strain.

Rodon, Jordi / Mykytyn, Anna Z / Te, Nigeer / Okba, Nisreen M A / Lamers, Mart M / Pailler-García, Lola / Cantero, Guillermo / Albulescu, Irina / Bosch, Berend-Jan / Peiris, Malik / Bensaid, Albert / Vergara-Alert, Júlia / Haagmans, Bart L / Segalés, Joaquim

Emerging infectious diseases

2023 Volume 29, Issue 3, Page(s) 585–589

Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) clade B viruses are found in camelids and humans in the Middle East, but clade C viruses are not. We provide experimental evidence for extended shedding of MERS-CoV clade B viruses in llamas, which ... ...

Abstract	Middle East respiratory syndrome coronavirus (MERS-CoV) clade B viruses are found in camelids and humans in the Middle East, but clade C viruses are not. We provide experimental evidence for extended shedding of MERS-CoV clade B viruses in llamas, which might explain why they outcompete clade C strains in the Arabian Peninsula.
MeSH term(s)	Animals ; Humans ; Middle East Respiratory Syndrome Coronavirus ; Camelids, New World ; Herpesvirus 1, Cercopithecine ; Coronavirus Infections ; Virus Shedding ; Camelus
Language	English
Publishing date	2023-02-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1380686-5
ISSN	1080-6059 ; 1080-6040
ISSN (online)	1080-6059
ISSN	1080-6040
DOI	10.3201/eid2903.220986
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4778: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Glycosylated extracellular mucin domains protect against SARS-CoV-2 infection at the respiratory surface.

Maitrayee Chatterjee / Liane Z X Huang / Anna Z Mykytyn / Chunyan Wang / Mart M Lamers / Bart Westendorp / Richard W Wubbolts / Jos P M van Putten / Berend-Jan Bosch / Bart L Haagmans / Karin Strijbis

PLoS Pathogens, Vol 19, Iss 8, p e

2023 Volume 1011571

Abstract	Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by mucociliary clearance. Transmembrane mucins MUC1, MUC4, and MUC16 can restrict microbial invasion at the apical surface of the epithelium. In this study, we determined the impact of host mucins and mucin glycans on epithelial entry of SARS-CoV-2. Human lung epithelial Calu-3 cells express the SARS-CoV-2 entry receptor ACE2 and high levels of glycosylated MUC1, but not MUC4 and MUC16, on their cell surface. The O-glycan-specific mucinase StcE specifically removed the glycosylated part of the MUC1 extracellular domain while leaving the underlying SEA domain and cytoplasmic tail intact. StcE treatment of Calu-3 cells significantly enhanced infection with SARS-CoV-2 pseudovirus and authentic virus, while removal of terminal mucin glycans sialic acid and fucose from the epithelial surface did not impact viral entry. In Calu-3 cells, the transmembrane mucin MUC1 and ACE2 are located to the apical surface in close proximity and StcE treatment results in enhanced binding of purified spike protein. Both MUC1 and MUC16 are expressed on the surface of human organoid-derived air-liquid interface (ALI) differentiated airway cultures and StcE treatment led to mucin removal and increased levels of SARS-CoV-2 replication. In these cultures, MUC1 was highly expressed in non-ciliated cells while MUC16 was enriched in goblet cells. In conclusion, the glycosylated extracellular domains of different transmembrane mucins might have similar protective functions in different respiratory cell types by restricting SARS-CoV-2 binding and entry.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2023-08-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Avidity engineering of human heavy-chain-only antibodies mitigates neutralization resistance of SARS-CoV-2 variants.

Du, Wenjuan / Janssens, Rick / Mykytyn, Anna Z / Li, Wentao / Drabek, Dubravka / van Haperen, Rien / Chatziandreou, Marianthi / Rissmann, Melanie / van der Lee, Joline / van Dortmondt, Melissa / Martin, Itziar Serna / van Kuppeveld, Frank J M / Hurdiss, Daniel L / Haagmans, Bart L / Grosveld, Frank / Bosch, Berend-Jan

Frontiers in immunology

2023 Volume 14, Page(s) 1111385

Abstract: Emerging SARS-CoV-2 variants have accrued mutations within the spike protein rendering most therapeutic monoclonal antibodies against COVID-19 ineffective. Hence there is an unmet need for broad-spectrum mAb treatments for COVID-19 that are more ... ...

Abstract	Emerging SARS-CoV-2 variants have accrued mutations within the spike protein rendering most therapeutic monoclonal antibodies against COVID-19 ineffective. Hence there is an unmet need for broad-spectrum mAb treatments for COVID-19 that are more resistant to antigenically drifted SARS-CoV-2 variants. Here we describe the design of a biparatopic heavy-chain-only antibody consisting of six antigen binding sites recognizing two distinct epitopes in the spike protein NTD and RBD. The hexavalent antibody showed potent neutralizing activity against SARS-CoV-2 and variants of concern, including the Omicron sub-lineages BA.1, BA.2, BA.4 and BA.5, whereas the parental components had lost Omicron neutralization potency. We demonstrate that the tethered design mitigates the substantial decrease in spike trimer affinity seen for escape mutations for the hexamer components. The hexavalent antibody protected against SARS-CoV-2 infection in a hamster model. This work provides a framework for designing therapeutic antibodies to overcome antibody neutralization escape of emerging SARS-CoV-2 variants.
MeSH term(s)	Animals ; Cricetinae ; Humans ; SARS-CoV-2/genetics ; COVID-19 ; Spike Glycoprotein, Coronavirus/genetics ; Immunoglobulin Heavy Chains/genetics ; Antibodies, Monoclonal
Chemical Substances	Spike Glycoprotein, Coronavirus ; Immunoglobulin Heavy Chains ; Antibodies, Monoclonal ; spike protein, SARS-CoV-2
Language	English
Publishing date	2023-02-21
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1111385
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Fangchinoline inhibits SARS-CoV-2 and MERS-CoV entry.

Sadhu, Srikanth / Dandotiya, Jyotsna / Dalal, Rajdeep / Khatri, Ritika / Mykytyn, Anna Z / Batra, Aashima / Kaur, Manpreet / Chandwaskar, Rucha / Singh, Virendra / Kamboj, Aarzoo / Srivastava, Mitul / Mani, Shailendra / Asthana, Shailendra / Samal, Sweety / Rizvi, Zaigham Abbas / Salunke, Deepak B / Haagmans, Bart L / Awasthi, Amit

Antiviral research

2023 Volume 220, Page(s) 105743

Abstract: The COVID-19 pandemic caused by SARS-CoV-2, lead to mild to severe respiratory illness and resulted in 6.9 million deaths worldwide. Although vaccines are effective in preventing COVID-19, they may not be sufficient to protect immunocompromised ... ...

Abstract	The COVID-19 pandemic caused by SARS-CoV-2, lead to mild to severe respiratory illness and resulted in 6.9 million deaths worldwide. Although vaccines are effective in preventing COVID-19, they may not be sufficient to protect immunocompromised individuals from this respiratory illness. Moreover, novel emerging variants of SARS-CoV-2 pose a risk of new COVID-19 waves. Therefore, identification of effective antivirals is critical in controlling SARS and other coronaviruses, such as MERS-CoV. We show that Fangchinoline (Fcn), a bisbenzylisoquinoline alkaloid, inhibits replication of SARS-CoV, SARS-CoV-2, and MERS-CoV in a range of in vitro assays, by blocking entry. Therapeutic use of Fcn inhibited viral loads in the lungs, and suppressed associated airway inflammation in hACE2. Tg mice and Syrian hamster infected with SARS-CoV-2. Combination of Fcn with remdesivir (RDV) or an anti-leprosy drug, Clofazimine, exhibited synergistic antiviral activity. Compared to Fcn, its synthetic derivative, MK-04-003, more effectively inhibited SARS-CoV-2 and its variants B.1.617.2 and BA.5 in mice. Taken together these data demonstrate that Fcn is a pan beta coronavirus inhibitor, which possibly can be used to combat novel emerging coronavirus diseases.
MeSH term(s)	Humans ; Mice ; Animals ; SARS-CoV-2 ; Middle East Respiratory Syndrome Coronavirus ; COVID-19 ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Pandemics ; Benzylisoquinolines/pharmacology ; Benzylisoquinolines/therapeutic use
Chemical Substances	fangchinoline (953592C3ZB) ; Antiviral Agents ; Benzylisoquinolines
Language	English
Publishing date	2023-11-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	306628-9
ISSN	1872-9096 ; 0166-3542
ISSN (online)	1872-9096
ISSN	0166-3542
DOI	10.1016/j.antiviral.2023.105743
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1627: 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: Protective efficacy of an RBD-based Middle East respiratory syndrome coronavirus (MERS-CoV) particle vaccine in llamas.

Rodon, Jordi / Mykytyn, Anna Z / Cantero, Guillermo / Albulescu, Irina C / Bosch, Berend-Jan / Brix, Alexander / Audonnet, Jean-Christophe / Bensaid, Albert / Vergara-Alert, Júlia / Haagmans, Bart L / Segalés, Joaquim

One health outlook

2022 Volume 4, Issue 1, Page(s) 12

Abstract: Ongoing outbreaks of Middle East respiratory syndrome coronavirus (MERS-CoV) continue posing a global health threat. Vaccination of livestock reservoir species is a recommended strategy to prevent spread of MERS-CoV among animals and potential spillover ... ...

Abstract	Ongoing outbreaks of Middle East respiratory syndrome coronavirus (MERS-CoV) continue posing a global health threat. Vaccination of livestock reservoir species is a recommended strategy to prevent spread of MERS-CoV among animals and potential spillover to humans. Using a direct-contact llama challenge model that mimics naturally occurring viral transmission, we tested the efficacy of a multimeric receptor binding domain (RBD) particle-display based vaccine candidate. While MERS-CoV was transmitted to naïve animals exposed to virus-inoculated llamas, immunization induced robust virus-neutralizing antibody responses and prevented transmission in 1/3 vaccinated, in-contact animals. Our exploratory study supports further improvement of the RBD-based vaccine to prevent zoonotic spillover of MERS-CoV.
Language	English
Publishing date	2022-06-24
Publishing country	England
Document type	Journal Article
ISSN	2524-4655
ISSN (online)	2524-4655
DOI	10.1186/s42522-022-00068-9
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

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

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

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

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