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2. Broadly neutralizing SARS-CoV-2 antibodies through epitope-based selection from convalescent patients

Author

Rouet, Romain, Henry, Jake Y., Johansen, Matt D., Sobti, Meghna, Balachandran, Harikrishnan, Langley, David B., Walker, Gregory J., Lenthall, Helen, Jackson, Jennifer, Ubiparipovic, Stephanie, Mazigi, Ohan, Schofield, Peter, Burnett, Deborah L., Brown, Simon H. J., Martinello, Marianne, Hudson, Bernard, Gilroy, Nicole, Post, Jeffrey J., Kelleher, Anthony, Jäck, Hans-Martin, Goodnow, Christopher C., Turville, Stuart G., Rawlinson, William D., Bull, Rowena A., Stewart, Alastair G., Hansbro, Philip M., and Christ, Daniel

Published
2023
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7. IRF4 deficiency vulnerates B-cell progeny for leukemogenesis via somatically acquired Jak3 mutations conferring IL-7 hypersensitivity

Author

Das Gupta, Dennis, Paul, Christoph, Samel, Nadine, Bieringer, Maria, Staudenraus, Daniel, Marini, Federico, Raifer, Hartmann, Menke, Lisa, Hansal, Lea, Camara, Bärbel, Roth, Edith, Daum, Patrick, Wanzel, Michael, Mernberger, Marco, Nist, Andrea, Bauer, Uta-Maria, Helmprobst, Frederik, Buchholz, Malte, Roth, Katrin, Bastian, Lorenz, Hartmann, Alina M., Baldus, Claudia, Ikuta, Koichi, Neubauer, Andreas, Burchert, Andreas, Jäck, Hans-Martin, Klein, Matthias, Bopp, Tobias, Stiewe, Thorsten, Pagenstecher, Axel, and Lohoff, Michael

Published
2022
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8. Platform for isolation and characterization of SARS-CoV-2 variants enables rapid characterization of Omicron in Australia

Author

Aggarwal, Anupriya, Stella, Alberto Ospina, Walker, Gregory, Akerman, Anouschka, Esneau, Camille, Milogiannakis, Vanessa, Burnett, Deborah L., McAllery, Samantha, Silva, Mariana Ruiz, Lu, Yonghui, Foster, Charles S. P., Brilot, Fabienne, Pillay, Aleha, Van Hal, Sabastiaan, Mathivanan, Vennila, Fichter, Christina, Kindinger, Andrea, Hoppe, Alexandra Carey, Munier, Mee Ling, Amatayakul-Chantler, Supavadee, Roth, Nathan, Coppola, Germano, Symonds, Geoff P., Schofield, Peter, Jackson, Jennifer, Lenthall, Helen, Henry, Jake Y., Mazigi, Ohan, Jäck, Hans-Martin, Davenport, Miles P., Darley, David R., Matthews, Gail V., Khoury, David S., Cromer, Deborah, Goodnow, Christopher C., Christ, Daniel, Robosa, Roselle, Starck, Damien J., Bartlett, Nathan W., Rawlinson, William D., Kelleher, Anthony D., and Turville, Stuart G.

Published
2022
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15. Immunizations with diverse sarbecovirus receptor-binding domains elicit SARS-CoV-2 neutralizing antibodies against a conserved site of vulnerability

Author

Burnett, Deborah L., Jackson, Katherine J.L., Langley, David B., Aggarwal, Anupriya, Stella, Alberto Ospina, Johansen, Matt D., Balachandran, Harikrishnan, Lenthall, Helen, Rouet, Romain, Walker, Gregory, Saunders, Bernadette M., Singh, Mandeep, Li, Hui, Henry, Jake Y., Jackson, Jennifer, Stewart, Alastair G., Witthauer, Franka, Spence, Matthew A., Hansbro, Nicole G., Jackson, Colin, Schofield, Peter, Milthorpe, Claire, Martinello, Marianne, Schulz, Sebastian R., Roth, Edith, Kelleher, Anthony, Emery, Sean, Britton, Warwick J., Rawlinson, William D., Karl, Rudolfo, Schäfer, Simon, Winkler, Thomas H., Brink, Robert, Bull, Rowena A., Hansbro, Philip M., Jäck, Hans-Martin, Turville, Stuart, Christ, Daniel, and Goodnow, Christopher C.

Published
2021
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17. SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies

Author

Hoffmann, Markus, Arora, Prerna, Groß, Rüdiger, Seidel, Alina, Hörnich, Bojan F., Hahn, Alexander S., Krüger, Nadine, Graichen, Luise, Hofmann-Winkler, Heike, Kempf, Amy, Winkler, Martin S., Schulz, Sebastian, Jäck, Hans-Martin, Jahrsdörfer, Bernd, Schrezenmeier, Hubert, Müller, Martin, Kleger, Alexander, Münch, Jan, and Pöhlmann, Stefan

Published
2021
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18. ACE2-independent sarbecovirus cell entry can be supported by TMPRSS2-related enzymes and can reduce sensitivity to antibody-mediated neutralization.

Author

Zhang, Lu, Cheng, Hsiu-Hsin, Krüger, Nadine, Hörnich, Bojan, Graichen, Luise, Hahn, Alexander S., Schulz, Sebastian R., Jäck, Hans-Martin, Stankov, Metodi V., Behrens, Georg M. N., Müller, Marcel A., Drosten, Christian, Mörer, Onnen, Winkler, Martin Sebastian, Qian, ZhaoHui, Pöhlmann, Stefan, and Hoffmann, Markus

Subjects
SERINE proteinases, HORSESHOE bats, CARRIER proteins, RACCOON dog, PROTEIN receptors
Abstract

The COVID-19 pandemic, caused by SARS-CoV-2, demonstrated that zoonotic transmission of animal sarbecoviruses threatens human health but the determinants of transmission are incompletely understood. Here, we show that most spike (S) proteins of horseshoe bat and Malayan pangolin sarbecoviruses employ ACE2 for entry, with human and raccoon dog ACE2 exhibiting broad receptor activity. The insertion of a multibasic cleavage site into the S proteins increased entry into human lung cells driven by most S proteins tested, suggesting that acquisition of a multibasic cleavage site might increase infectivity of diverse animal sarbecoviruses for the human respiratory tract. In contrast, two bat sarbecovirus S proteins drove cell entry in an ACE2-independent, trypsin-dependent fashion and several ACE2-dependent S proteins could switch to the ACE2-independent entry pathway when exposed to trypsin. Several TMPRSS2-related cellular proteases but not the insertion of a multibasic cleavage site into the S protein allowed for ACE2-independent entry in the absence of trypsin and may support viral spread in the respiratory tract. Finally, the pan-sarbecovirus antibody S2H97 enhanced cell entry driven by two S proteins and this effect was reversed by trypsin while trypsin protected entry driven by a third S protein from neutralization by S2H97. Similarly, plasma from quadruple vaccinated individuals neutralized entry driven by all S proteins studied, and availability of the ACE2-independent, trypsin-dependent pathway reduced neutralization sensitivity. In sum, our study reports a pathway for entry into human cells that is ACE2-independent, can be supported by TMPRSS2-related proteases and may be associated with antibody evasion. Author summary: Bats host a wide range of coronaviruses, including those related to SARS-CoV-1 and SARS-CoV-2 (subgenus Sarbecovirus), but their ability to infect human cells remains poorly understood. Identifying sarbecoviruses with zoonotic potential and understanding the factors controlling their entry into human cells are crucial for risk assessment and antiviral development. In this study, we examined how bat sarbecovirus spike proteins facilitate entry into human cells and identified key host factors involved. Using pseudovirus particles, we show that several bat sarbecovirus spike proteins use human and animal ACE2 receptors for entry. Additionally, we confirm that some spike proteins utilize an ACE2-independent entry pathway requiring trypsin treatment and demonstrate that this process is controlled by the spike protein receptor binding domain. Furthermore, we reveal that a subset of ACE2-using bat sarbecovirus spike proteins can switch to ACE2-independent entry following trypsin exposure and show that certain human type II transmembrane serine proteases can substitute for trypsin, enabling ACE2-independent entry. Finally, we demonstrate that repeated COVID-19 vaccination generates cross-neutralizing activity against bat sarbecoviruses, though ACE2-independent entry reduces neutralization sensitivity. [ABSTRACT FROM AUTHOR]

Published
2024
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19. Comparative Analysis of Host Cell Entry Efficiency and Neutralization Sensitivity of Emerging SARS-CoV-2 Lineages KP.2, KP.2.3, KP.3, and LB.1.

Author

Chen, Nianzhen, Decker, Katharina Emma, Schulz, Sebastian R., Kempf, Amy, Nehlmeier, Inga, Moldenhauer, Anna-Sophie, Dopfer-Jablonka, Alexandra, Behrens, Georg M. N., Stankov, Metodi V., Manthey, Luis, Jäck, Hans-Martin, Hoffmann, Markus, Pöhlmann, Stefan, and Arora, Prerna

Subjects
SARS-CoV-2 Omicron variant, ANGIOTENSIN converting enzyme, ANIMAL species, CELL analysis, SARS-CoV-2
Abstract

New SARS-CoV-2 lineages continue to evolve and may exhibit new characteristics regarding host cell entry efficiency and potential for antibody evasion. Here, employing pseudotyped particles, we compared the host cell entry efficiency, ACE2 receptor usage, and sensitivity to antibody-mediated neutralization of four emerging SARS-CoV-2 lineages, KP.2, KP.2.3, KP.3, and LB.1. The XBB.1.5 and JN.1 lineages served as controls. Our findings reveal that KP.2, KP.2.3, KP.3, and LB.1 lineages enter host cells efficiently and in an ACE2-dependent manner, and that KP.3 is more adept at entering Calu-3 lung cells than JN.1. However, the variants differed in their capacity to employ ACE2 orthologues from animal species for entry, suggesting differences in ACE2 interactions. Moreover, we demonstrate that only two out of seven therapeutic monoclonal antibody (mAbs) in preclinical development retain robust neutralizing activity against the emerging JN.1 sublineages tested, while three mAbs displayed strongly reduced neutralizing activity and two mAbs lacked neutralizing activity against any of the lineages tested. Furthermore, our results show that KP.2, KP.2.3, KP.3, and LB.1 lineages evade neutralization by antibodies induced by infection or vaccination with greater efficiency than JN.1, particularly in individuals without hybrid immunity. This study indicates that KP.2, KP.2.3, KP.3, and LB.1 differ in ACE2 interactions and the efficiency of lung cell entry and suggest that evasion of neutralizing antibodies drove the emergence of these variants. [ABSTRACT FROM AUTHOR]

Published
2024
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20. An Enhanced Retroviral Vector for Efficient Genetic Manipulation and Selection in Mammalian Cells.

Author

Triller, Jana, Prots, Iryna, Jäck, Hans-Martin, and Wittmann, Jürgen

Subjects
GENETIC vectors, MOUSE leukemia viruses, RETROVIRUS diseases, CHIMERIC proteins, B cells
Abstract

Introducing genetic material into hard-to-transfect mammalian cell lines and primary cells is often best achieved through retroviral infection. An ideal retroviral vector should offer a compact, selectable, and screenable marker while maximizing transgene delivery capacity. However, a previously published retroviral vector featuring an EGFP/Puromycin fusion protein failed to meet these criteria in our experiments. We encountered issues such as low infection efficiency, weak EGFP fluorescence, and selection against infected cells. To address these shortcomings, we developed a novel retroviral vector based on the Moloney murine leukemia virus. This vector includes a compact bifunctional EGFP and Puromycin resistance cassette connected by a 2A peptide. Our extensively tested vector demonstrated superior EGFP expression, efficient Puromycin selection, and no growth penalty in infected cells compared with the earlier design. These benefits were consistent across multiple mammalian cell types, underscoring the versatility of our vector. In summary, our enhanced retroviral vector offers a robust solution for efficient infection, reliable detection, and effective selection in mammalian cells. Its improved performance and compact design make it an ideal choice for a wide range of applications involving precise genetic manipulation and characterization in cell-based studies. [ABSTRACT FROM AUTHOR]

Published
2024
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22. Virological Traits of the SARS-CoV-2 BA.2.87.1 Lineage

Author

Zhang, Lu, primary, Dopfer-Jablonka, Alexandra, additional, Nehlmeier, Inga, additional, Kempf, Amy, additional, Graichen, Luise, additional, Calderón Hampel, Noemí, additional, Cossmann, Anne, additional, Stankov, Metodi V., additional, Morillas Ramos, Gema, additional, Schulz, Sebastian R., additional, Jäck, Hans-Martin, additional, Behrens, Georg M. N., additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2024
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24. APOBEC3 enzymes restrict marginal zone B cells

Author

Beck‐Engeser, Gabriele B, Winkelmann, Rebecca, Wheeler, Matthew L, Shansab, Maryam, Yu, Philipp, Wünsche, Sarah, Walchhütter, Anja, Metzner, Mirjam, Vettermann, Christian, Eilat, Dan, DeFranco, Anthony, Jäck, Hans‐Martin, and Wabl, Matthias

Subjects
Medical Microbiology, Biomedical and Clinical Sciences, Immunology, Biotechnology, Immunization, Infectious Diseases, Aetiology, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Underpinning research, Good Health and Well Being, APOBEC Deaminases, Animals, Antibody Formation, B-Lymphocytes, Cytidine Deaminase, Cytosine Deaminase, Germinal Center, Humans, Mice, Mice, Inbred BALB C, Mice, Knockout, Virus Diseases, Apobec3, B cell, Hitchhiker-1, Recovery from Friend virus 3, Sialyl transferases
Abstract

In general, a long-lasting immune response to viruses is achieved when they are infectious and replication competent. In the mouse, the neutralizing antibody response to Friend murine leukemia virus is contributed by an allelic form of the enzyme Apobec3 (abbreviated A3). This is counterintuitive because A3 directly controls viremia before the onset of adaptive antiviral immune responses. It suggests that A3 also affects the antibody response directly. Here, we studied the relative size of cell populations of the adaptive immune system as a function of A3 activity. We created a transgenic mouse that expresses all seven human A3 enzymes and compared it to WT and mouse A3-deficient mice. A3 enzymes decreased the number of marginal zone B cells, but not the number of follicular B or T cells. When mouse A3 was knocked out, the retroelement hitchhiker-1 and sialyl transferases encoded by genes close to it were overexpressed three and two orders of magnitude, respectively. We suggest that A3 shifts the balance, from the fast antibody response mediated by marginal zone B cells with little affinity maturation, to a more sustained germinal center B-cell response, which drives affinity maturation and, thereby, a better neutralizing response.

Published
2015

29. BCL6 is critical for the development of a diverse primary B cell repertoire

Author

Duy, Cihangir, Yu, J Jessica, Nahar, Rahul, Swaminathan, Srividya, Kweon, Soo-Mi, Polo, Jose M, Valls, Ester, Klemm, Lars, Shojaee, Seyedmehdi, Cerchietti, Leandro, Schuh, Wolfgang, Jäck, Hans-Martin, Hurtz, Christian, Ramezani-Rad, Parham, Herzog, Sebastian, Jumaa, Hassan, Koeffler, H Phillip, de Alborán, Ignacio Moreno, Melnick, Ari M, Ye, B Hilda, and Müschen, Markus

Subjects
Biomedical and Clinical Sciences, Stem Cell Research - Nonembryonic - Non-Human, Genetics, Stem Cell Research, Aetiology, Underpinning research, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, ADP-Ribosylation Factors, Animals, Apoptosis, B-Lymphocytes, Base Sequence, Cell Proliferation, Cell Survival, Cells, Cultured, Cytoprotection, DNA Damage, DNA-Binding Proteins, Down-Regulation, Gene Rearrangement, B-Lymphocyte, Light Chain, Humans, Interleukin-7, Lymphopoiesis, Mice, Molecular Sequence Data, Pre-B Cell Receptors, Precursor Cells, B-Lymphoid, Proto-Oncogene Proteins c-bcl-6, Proto-Oncogene Proteins c-myc, Recombination, Genetic, Signal Transduction, Transcription, Genetic, Up-Regulation, Medical and Health Sciences, Immunology, Biomedical and clinical sciences, Health sciences
Abstract

BCL6 protects germinal center (GC) B cells against DNA damage-induced apoptosis during somatic hypermutation and class-switch recombination. Although expression of BCL6 was not found in early IL-7-dependent B cell precursors, we report that IL-7Ralpha-Stat5 signaling negatively regulates BCL6. Upon productive VH-DJH gene rearrangement and expression of a mu heavy chain, however, activation of pre-B cell receptor signaling strongly induces BCL6 expression, whereas IL-7Ralpha-Stat5 signaling is attenuated. At the transition from IL-7-dependent to -independent stages of B cell development, BCL6 is activated, reaches expression levels resembling those in GC B cells, and protects pre-B cells from DNA damage-induced apoptosis during immunoglobulin (Ig) light chain gene recombination. In the absence of BCL6, DNA breaks during Ig light chain gene rearrangement lead to excessive up-regulation of Arf and p53. As a consequence, the pool of new bone marrow immature B cells is markedly reduced in size and clonal diversity. We conclude that negative regulation of Arf by BCL6 is required for pre-B cell self-renewal and the formation of a diverse polyclonal B cell repertoire.

Published
2010

31. Neutralisation sensitivity of SARS-CoV-2 lineages EG.5.1 and XBB.2.3

Author

Zhang, Lu, primary, Kempf, Amy, additional, Nehlmeier, Inga, additional, Cossmann, Anne, additional, Dopfer-Jablonka, Alexandra, additional, Stankov, Metodi V, additional, Schulz, Sebastian R, additional, Jäck, Hans-Martin, additional, Behrens, Georg M N, additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2023
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36. The intestine: A highly dynamic microenvironment for IgA plasma cells

Author

Pracht, Katharina, Wittner, Jens, Kagerer, Fritz, Jäck, Hans-Martin, and Schuh, Wolfgang

Subjects
Immunology, Immunology and Allergy, ddc:610
Abstract

To achieve longevity, IgA plasma cells require a sophisticated anatomical microenvironment that provides cytokines, cell-cell contacts, and nutrients as well as metabolites. The intestinal epithelium harbors cells with distinct functions and represents an important defense line. Anti-microbial peptide-producing paneth cells, mucus-secreting goblet cells and antigen-transporting microfold (M) cells cooperate to build a protective barrier against pathogens. In addition, intestinal epithelial cells are instrumental in the transcytosis of IgA to the gut lumen, and support plasma cell survival by producing the cytokines APRIL and BAFF. Moreover, nutrients are sensed through specialized receptors such as the aryl hydrocarbon receptor (AhR) by both, intestinal epithelial cells and immune cells. However, the intestinal epithelium is highly dynamic with a high cellular turn-over rate and exposure to changing microbiota and nutritional factors. In this review, we discuss the spatial interplay of the intestinal epithelium with plasma cells and its potential contribution to IgA plasma cell generation, homing, and longevity. Moreover, we describe the impact of nutritional AhR ligands on intestinal epithelial cell-IgA plasma cell interaction. Finally, we introduce spatial transcriptomics as a new technology to address open questions in intestinal IgA plasma cell biology.

Published
2023
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37. Neutralisation sensitivity of the SARS-CoV-2 XBB.1 lineage

Author

Arora, Prerna, primary, Cossmann, Anne, additional, Schulz, Sebastian R, additional, Ramos, Gema Morillas, additional, Stankov, Metodi V, additional, Jäck, Hans-Martin, additional, Behrens, Georg M N, additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2023
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40. The effect of cilgavimab and neutralisation by vaccine-induced antibodies in emerging SARS-CoV-2 BA.4 and BA.5 sublineages

Author

Arora, Prerna, primary, Zhang, Lu, additional, Nehlmeier, Inga, additional, Kempf, Amy, additional, Cossmann, Anne, additional, Dopfer-Jablonka, Alexandra, additional, Schulz, Sebastian R, additional, Jäck, Hans-Martin, additional, Behrens, Georg M N, additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2022
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41. Host Cell Entry and Neutralization Sensitivity of SARS-CoV-2 Lineages B.1.620 and R.1

Author

Sidarovich, Anzhalika, primary, Krüger, Nadine, additional, Rocha, Cheila, additional, Graichen, Luise, additional, Kempf, Amy, additional, Nehlmeier, Inga, additional, Lier, Martin, additional, Cossmann, Anne, additional, Stankov, Metodi V., additional, Schulz, Sebastian R., additional, Behrens, Georg M. N., additional, Jäck, Hans-Martin, additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2022
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42. Lung cell entry, cell–cell fusion capacity, and neutralisation sensitivity of omicron sublineage BA.2.75

Author

Arora, Prerna, primary, Nehlmeier, Inga, additional, Kempf, Amy, additional, Cossmann, Anne, additional, Schulz, Sebastian R, additional, Dopfer-Jablonka, Alexandra, additional, Baier, Eva, additional, Tampe, Björn, additional, Moerer, Onnen, additional, Dickel, Steffen, additional, Winkler, Martin S, additional, Jäck, Hans-Martin, additional, Behrens, Georg M N, additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2022
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43. Broadly neutralizing SARS-CoV-2 antibodies through epitope-based selection from convalescent patients

Author

Rouet, Romain, primary, Henry, Jake Y., additional, Johansen, Matt D., additional, Sobti, Meghna, additional, Balachandran, Harikrishnan, additional, Langley, David B., additional, Walker, Gregory, additional, Lenthall, Helen, additional, Jackson, Jennifer, additional, Ubiparipovic, Stephanie, additional, Mazigi, Ohan, additional, Schofield, Peter, additional, Burnett, Deborah L., additional, Brown, Simon H. J., additional, Martinello, Marianne, additional, Hudson, Bernard, additional, Gilroy, Nicole, additional, Post, Jeffrey J., additional, Kelleher, Anthony, additional, Jäck, Hans-Martin, additional, Goodnow, Christopher C., additional, Turville, Stuart G., additional, Rawlinson, William D., additional, Bull, Rowena A., additional, Stewart, Alastair G., additional, Hansbro, Philip M., additional, and Christ, Daniel, additional

Published
2022
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46. Evidence for an ACE2-Independent Entry Pathway That Can Protect from Neutralization by an Antibody Used for COVID-19 Therapy

Author

Hoffmann, Markus, primary, Sidarovich, Anzhalika, additional, Arora, Prerna, additional, Krüger, Nadine, additional, Nehlmeier, Inga, additional, Kempf, Amy, additional, Graichen, Luise, additional, Winkler, Martin S., additional, Niemeyer, Daniela, additional, Goffinet, Christine, additional, Drosten, Christian, additional, Schulz, Sebastian, additional, Jäck, Hans-Martin, additional, and Pöhlmann, Stefan, additional

Published
2022
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47. Comparable neutralisation evasion of SARS-CoV-2 omicron subvariants BA.1, BA.2, and BA.3

Author

Arora, Prerna, primary, Zhang, Lu, additional, Rocha, Cheila, additional, Sidarovich, Anzhalika, additional, Kempf, Amy, additional, Schulz, Sebastian, additional, Cossmann, Anne, additional, Manger, Bernhard, additional, Baier, Eva, additional, Tampe, Björn, additional, Moerer, Onnen, additional, Dickel, Steffen, additional, Dopfer-Jablonka, Alexandra, additional, Jäck, Hans-Martin, additional, Behrens, Georg M N, additional, Winkler, Martin S, additional, Pöhlmann, Stefan, additional, and Hoffmann, Markus, additional

Published
2022
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