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Article ; Online: Isolation and Characterization of Neutralizing Monoclonal Antibodies from a Large Panel of Murine Antibodies against RBD of the SARS-CoV-2 Spike Protein.

D'Acunto, Emanuela / Muzi, Alessia / Marchese, Silvia / Donnici, Lorena / Chiarini, Valerio / Bucci, Federica / Pavoni, Emiliano / Ferrara, Fabiana Fosca / Cappelletti, Manuela / Arriga, Roberto / Serrao, Silvia Maria / Peluzzi, Valentina / Principato, Eugenia / Compagnone, Mirco / Pinto, Eleonora / Luberto, Laura / Stoppoloni, Daniela / Lahm, Armin / Groß, Rüdiger /

Seidel, Alina / Wettstein, Lukas / Münch, Jan / Goodhead, Andrew / Parisot, Judicael / De Francesco, Raffaele / Ciliberto, Gennaro / Marra, Emanuele / Aurisicchio, Luigi / Roscilli, Giuseppe

Antibodies (Basel, Switzerland)

2024 Volume 13, Issue 1

Abstract: The COVID-19 pandemic, once a global crisis, is now largely under control, a testament to the extraordinary global efforts involving vaccination and public health measures. However, the relentless evolution of SARS-CoV-2, leading to the emergence of new ... ...

Abstract	The COVID-19 pandemic, once a global crisis, is now largely under control, a testament to the extraordinary global efforts involving vaccination and public health measures. However, the relentless evolution of SARS-CoV-2, leading to the emergence of new variants, continues to underscore the importance of remaining vigilant and adaptable. Monoclonal antibodies (mAbs) have stood out as a powerful and immediate therapeutic response to COVID-19. Despite the success of mAbs, the evolution of SARS-CoV-2 continues to pose challenges and the available antibodies are no longer effective. New variants require the ongoing development of effective antibodies. In the present study, we describe the generation and characterization of neutralizing mAbs against the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein by combining plasmid DNA and recombinant protein vaccination. By integrating genetic immunization for rapid antibody production and the potent immune stimulation enabled by protein vaccination, we produced a rich pool of antibodies, each with unique binding and neutralizing specificities, tested with the ELISA, BLI and FACS assays and the pseudovirus assay, respectively. Here, we present a panel of mAbs effective against the SARS-CoV-2 variants up to Omicron BA.1 and BA.5, with the flexibility to target emerging variants. This approach ensures the preparedness principle is in place to address SARS-CoV-2 actual and future infections.
Language	English
Publishing date	2024-01-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661514-9
ISSN	2073-4468 ; 2073-4468
ISSN (online)	2073-4468
ISSN	2073-4468
DOI	10.3390/antib13010005
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Article ; Online: Optimized selection of anti-tumor recombinant antibodies from phage libraries on intact cells.

Pavoni, Emiliano / Vaccaro, Paola / Anastasi, Anna Maria / Minenkova, Olga

Molecular immunology

2014 Volume 57, Issue 2, Page(s) 317–322

Abstract: Generation of human recombinant antibody libraries displayed on the surface of the filamentous phage and selection of specific antibodies against desirable targets allows production of fully human antibodies usable for repeated administration in humans. ... ...

Abstract	Generation of human recombinant antibody libraries displayed on the surface of the filamentous phage and selection of specific antibodies against desirable targets allows production of fully human antibodies usable for repeated administration in humans. Various lymphoid tissues from immunized donors, such as lymph nodes or peripheral blood lymphocytes from individuals with tumor or lymphocytes infiltrating tumor masses may serve as a source of specific anti-tumor antibody repertoire for generation of tumor-focused phage display libraries. In the case of lack of tumor-associated antigens in the purified form, high affinity anti-tumor antibodies can be isolated through library panning on whole cells expressing these antigens. However, affinity selection against cell surface specific antigens within highly heterogeneous population of molecules is not a very efficient process that often results in the selection of unspecific antibodies or antibodies against intracellular antigens that are generally useless for targeted immunotherapy. In this work, we developed a new cell-based antibody selection protocol that, by eliminating the contamination of dead cells from the cell suspension, dramatically improves the selection frequency of anti-tumor antibodies recognizing cell surface antigens.
MeSH term(s)	Antibodies, Anti-Idiotypic/genetics ; Antibodies, Anti-Idiotypic/immunology ; Antibodies, Neoplasm/genetics ; Antibodies, Neoplasm/immunology ; Antibodies, Neoplasm/isolation & purification ; Antigens, Neoplasm/immunology ; Antigens, Surface/immunology ; Cell Line, Tumor ; Female ; Humans ; Immunoglobulin Variable Region/genetics ; Immunoglobulin Variable Region/immunology ; MCF-7 Cells ; Peptide Library ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Recombinant Proteins/isolation & purification ; Single-Chain Antibodies/immunology
Chemical Substances	Antibodies, Anti-Idiotypic ; Antibodies, Neoplasm ; Antigens, Neoplasm ; Antigens, Surface ; Immunoglobulin Variable Region ; Peptide Library ; Recombinant Proteins ; Single-Chain Antibodies
Language	English
Publishing date	2014-02
Publishing country	England
Document type	Journal Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2013.10.009
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Article ; Online: New classes of potent heparanase inhibitors from ligand-based virtual screening.

Pala, Daniele / Scalvini, Laura / Elisi, Gian Marco / Lodola, Alessio / Mor, Marco / Spadoni, Gilberto / Ferrara, Fabiana F / Pavoni, Emiliano / Roscilli, Giuseppe / Milazzo, Ferdinando M / Battistuzzi, Gianfranco / Rivara, Silvia / Giannini, Giuseppe

Journal of enzyme inhibition and medicinal chemistry

2020 Volume 35, Issue 1, Page(s) 1685–1696

Abstract: Heparanase is a validated target in cancer therapy and a potential target for several inflammatory pathologies. A ligand-based virtual screening of commercial libraries was performed to expand the chemical space of small-molecule inhibitors. The ... ...

Abstract	Heparanase is a validated target in cancer therapy and a potential target for several inflammatory pathologies. A ligand-based virtual screening of commercial libraries was performed to expand the chemical space of small-molecule inhibitors. The screening was based on similarity with known inhibitors and was performed in several runs, starting from literature compounds and progressing through newly discovered inhibitors. Among the fifty-five tested compounds, nineteen had IC
MeSH term(s)	Amides/chemistry ; Amides/pharmacology ; Dose-Response Relationship, Drug ; Drug Evaluation, Preclinical ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Glucuronidase/antagonists & inhibitors ; Glucuronidase/metabolism ; Humans ; Ligands ; Models, Molecular ; Molecular Structure ; Structure-Activity Relationship
Chemical Substances	Amides ; Enzyme Inhibitors ; Ligands ; heparanase (EC 3.2.1.-) ; Glucuronidase (EC 3.2.1.31)
Language	English
Publishing date	2020-09-09
Publishing country	England
Document type	Journal Article
ZDB-ID	2082578-X
ISSN	1475-6374 ; 1475-6366
ISSN (online)	1475-6374
ISSN	1475-6366
DOI	10.1080/14756366.2020.1811701
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Article: Optimized selection of anti-tumor recombinant antibodies from phage libraries on intact cells

Pavoni, Emiliano / Anna Maria Anastasi / Olga Minenkova / Paola Vaccaro

Molecular Immunology. 2014 Feb., v. 57

2014

Abstract	Generation of human recombinant antibody libraries displayed on the surface of the filamentous phage and selection of specific antibodies against desirable targets allows production of fully human antibodies usable for repeated administration in humans. Various lymphoid tissues from immunized donors, such as lymph nodes or peripheral blood lymphocytes from individuals with tumor or lymphocytes infiltrating tumor masses may serve as a source of specific anti-tumor antibody repertoire for generation of tumor-focused phage display libraries. In the case of lack of tumor-associated antigens in the purified form, high affinity anti-tumor antibodies can be isolated through library panning on whole cells expressing these antigens. However, affinity selection against cell surface specific antigens within highly heterogeneous population of molecules is not a very efficient process that often results in the selection of unspecific antibodies or antibodies against intracellular antigens that are generally useless for targeted immunotherapy.In this work, we developed a new cell-based antibody selection protocol that, by eliminating the contamination of dead cells from the cell suspension, dramatically improves the selection frequency of anti-tumor antibodies recognizing cell surface antigens.
Keywords	bacteriophages ; DNA libraries ; humans ; lymph nodes ; lymphocytes ; peptide libraries ; recombinant antibodies ; surface antigens ; tissues
Language	English
Dates of publication	2014-02
Size	p. 317-322.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2013.10.009
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Article ; Online: The natural compound fucoidan from New Zealand Undaria pinnatifida synergizes with the ERBB inhibitor lapatinib enhancing melanoma growth inhibition.

Thakur, Varsha / Lu, Jun / Roscilli, Giuseppe / Aurisicchio, Luigi / Cappelletti, Manuela / Pavoni, Emiliano / White, William Lindsey / Bedogni, Barbara

Oncotarget

2017 Volume 8, Issue 11, Page(s) 17887–17896

Abstract: Melanoma remains one of the most aggressive and therapy-resistant cancers. Finding new treatments to improve patient outcomes is an ongoing effort. We previously demonstrated that melanoma relies on the activation of ERBB signaling, specifically of the ... ...

Abstract	Melanoma remains one of the most aggressive and therapy-resistant cancers. Finding new treatments to improve patient outcomes is an ongoing effort. We previously demonstrated that melanoma relies on the activation of ERBB signaling, specifically of the ERBB3/ERBB2 cascade. Here we show that melanoma tumor growth is inhibited by 60% over controls when treated with lapatinib, a clinically approved inhibitor of ERBB2/EGFR. Importantly, tumor growth is further inhibited to 85% when the natural compound fucoidan from New Zealand U. pinnatifida is integrated into the treatment regimen. Fucoidan not only enhances tumor growth inhibition, it counteracts the morbidity associated with prolonged lapatinib treatment. Fucoidan doubles the cell killing capacity of lapatinib. These effects are associated with a further decrease in AKT and NFκB signaling, two key pathways involved in melanoma cell survival. Importantly, the enhancing cell killing effects of fucoidan can be recapitulated by inhibiting ERBB3 by either a specific shRNA or a novel, selective ERBB3 neutralizing antibody, reiterating the key roles played by this receptor in melanoma. We therefore propose the use of lapatinib or specific ERBB inhibitors, in combination with fucoidan as a new treatment of melanoma that potentiates the effects of the inhibitors while protecting from their potential side effects.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Combined Chemotherapy Protocols/pharmacology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Drug Synergism ; ErbB Receptors/antagonists & inhibitors ; Humans ; Lapatinib ; Male ; Melanoma/drug therapy ; Melanoma/metabolism ; Mice ; Mice, SCID ; New Zealand ; Polysaccharides/pharmacology ; Proto-Oncogene Proteins c-akt/metabolism ; Quinazolines/pharmacology ; RNA Interference ; RNA, Small Interfering/genetics ; Receptor, ErbB-2/antagonists & inhibitors ; Receptor, ErbB-2/metabolism ; Receptor, ErbB-3/antagonists & inhibitors ; Receptor, ErbB-3/genetics ; Receptor, ErbB-3/metabolism ; Transcription Factor RelA/metabolism ; Undaria/chemistry
Chemical Substances	Antineoplastic Agents ; Polysaccharides ; Quinazolines ; RELA protein, human ; RNA, Small Interfering ; Transcription Factor RelA ; Lapatinib (0VUA21238F) ; fucoidan (9072-19-9) ; EGFR protein, human (EC 2.7.10.1) ; ERBB2 protein, human (EC 2.7.10.1) ; ERBB3 protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1) ; Receptor, ErbB-3 (EC 2.7.10.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2017-02-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.14437
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Article ; Online: Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase.

Pala, Daniele / Rivara, Silvia / Mor, Marco / Milazzo, Ferdinando Maria / Roscilli, Giuseppe / Pavoni, Emiliano / Giannini, Giuseppe

Glycobiology

2016 Volume 26, Issue 6, Page(s) 640–654

Abstract: Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making ... ...

Abstract	Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making heparanase an attractive target for the development of anticancer therapies. SST0001 (roneparstat; Sigma-Tau Research Switzerland S.A.) is a non-anticoagulant 100% N-acetylated and glycol-split heparin acting as a potent heparanase inhibitor, currently in phase I in advanced multiple myeloma. Herein, the kinetics of heparanase inhibition by roneparstat is reported. The analysis of dose-inhibition curves confirmed the high potency of roneparstat (IC50 ≈ 3 nM) and showed, at higher concentrations, a Hill coefficient consistent with the engagement of two molecules of inhibitor. A homology model of human heparanase GS3 construct was built and used for docking experiments with inhibitor fragments. The model has high structural similarity with the recently reported crystal structure of human heparanase. Different interaction schemes are proposed, which support the hypothesis of a complex binding mechanism involving the recruitment of one or multiple roneparstat chains, depending on its concentration. In particular, docking solutions were obtained in which (i) a single roneparstat molecule interacts with both heparin-binding domains (HBDs) of heparanase or (ii) two fragments of roneparstat interact with either HBD-1 or HBD-2, consistent with the possibility of different inhibitor:enzyme binding stoichiometries. This study provides unique insights into the mode of action of roneparstat as well as clues of its interaction with heparanase at a molecular level, which could be exploited to design novel potential inhibitor molecules.
Language	English
Publishing date	2016-06
Publishing country	England
Document type	Journal Article
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cww003
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Article ; Online: Simultaneous display of two large proteins on the head and tail of bacteriophage lambda.

Pavoni, Emiliano / Vaccaro, Paola / D'Alessio, Valeria / De Santis, Rita / Minenkova, Olga

BMC biotechnology

2013 Volume 13, Page(s) 79

Abstract: Background: Consistent progress in the development of bacteriophage lambda display platform as an alternative to filamentous phage display system was achieved in the recent years. The lambda phage has been engineered to display efficiently multiple ... ...

Abstract	Background: Consistent progress in the development of bacteriophage lambda display platform as an alternative to filamentous phage display system was achieved in the recent years. The lambda phage has been engineered to display efficiently multiple copies of peptides or even large protein domains providing a powerful tool for screening libraries of peptides, proteins and cDNA. Results: In the present work we describe an original method for dual display of large proteins on the surface of lambda particles. An anti-CEA single-chain antibody fragment and green fluorescent protein or alkaline phosphatase were simultaneously displayed by engineering both gpD and gpV lambda proteins. Conclusions: Here we show that such modified phage particles can be used for the detection of target molecules in vitro and in vivo. Dual expression of functional moieties on the surface of the lambda phage might open the way to generation of a new class of diagnostic and therapeutic targeted nanoparticles.
MeSH term(s)	Alkaline Phosphatase/metabolism ; Animals ; Bacteriophage lambda/genetics ; Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Cell Line ; Cloning, Molecular ; DNA, Complementary/chemistry ; DNA, Complementary/genetics ; Escherichia coli/genetics ; Genetic Vectors ; Glycoproteins/chemistry ; Glycoproteins/genetics ; Green Fluorescent Proteins/genetics ; HT29 Cells ; Humans ; Mice ; Mice, Nude ; Microscopy, Confocal ; Nanoparticles/chemistry ; Peptide Library ; Plasmids/genetics ; Protein Structure, Tertiary ; Proteins/chemistry ; Proteins/genetics ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Capsid Proteins ; DNA, Complementary ; Glycoproteins ; Peptide Library ; Proteins ; Recombinant Fusion Proteins ; gpD protein, lambda phage ; Green Fluorescent Proteins (147336-22-9) ; Alkaline Phosphatase (EC 3.1.3.1)
Language	English
Publishing date	2013-09-30
Publishing country	England
Document type	Journal Article
ZDB-ID	2052746-9
ISSN	1472-6750 ; 1472-6750
ISSN (online)	1472-6750
ISSN	1472-6750
DOI	10.1186/1472-6750-13-79
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Article: New display vector reduces biological bias for expression of antibodies in E. coli.

Pavoni, Emiliano / Monteriù, Giorgia / Cianfriglia, Maurizio / Minenkova, Olga

Gene

2007 Volume 391, Issue 1-2, Page(s) 120–129

Abstract: We report the development of a novel phagemid vector, pKM19, for display of recombinant antibodies in single-chain format (scFv) on the surface of filamentous phage. This new vector improves efficacy of selection and reduces the biological bias against ... ...

Abstract	We report the development of a novel phagemid vector, pKM19, for display of recombinant antibodies in single-chain format (scFv) on the surface of filamentous phage. This new vector improves efficacy of selection and reduces the biological bias against antibodies that can be harmful to host bacteria. It is useful for generation of large new antibody libraries, and for the subsequent maturation of antibody fragments. In comparison with commonly used plasmids, this vector is designed to have relatively low expression levels of cloned scFv antibodies due to the amber codon positioned in a sequence encoding for the PhoA leader peptide. Moreover, fusion of antibodies to the carboxy terminal part only of the gene III protein improves display of scFv on bacteriophage surface in this system. Despite the lower antibody expression, the functional test performed with a new scFv library derived from human peripheral blood lymphocytes demonstrates that specific antibodies can be easily isolated from the library, even after the second selection round. The use of the pKM19 vector for maturation of an anti-CEA antibody significantly improves the final results. In our previous work, an analogous selection through the use of a phagemid vector, with antibody expression under the control of a lacP promoter, led to isolation of anti-CEA phage antibodies with improved affinities, which were not producible in soluble form. Probably due to the toxicity for E. coli of that particular anti-CEA antibody, 70% of maturated clones contained suppressed stop codons, acquired during various selection/amplification rounds. The pKM19 plasmid facilitates an efficient maturation process, resulting in selection of antibodies with improved affinity without any stop codons.
MeSH term(s)	Antibodies/genetics ; Antibodies/immunology ; Antibodies/metabolism ; Antibody Affinity ; Carcinoembryonic Antigen/immunology ; Enzyme-Linked Immunosorbent Assay ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Gene Library ; Genetic Vectors/genetics ; Humans ; Immunoglobulin Fc Fragments/immunology ; Inovirus/genetics ; Inovirus/metabolism ; Protein Binding ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/immunology
Chemical Substances	Antibodies ; Carcinoembryonic Antigen ; Immunoglobulin Fc Fragments ; Recombinant Proteins
Language	English
Publishing date	2007-04-15
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	391792-7
ISSN	1879-0038 ; 0378-1119
ISSN (online)	1879-0038
ISSN	0378-1119
DOI	10.1016/j.gene.2006.12.009
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Article ; Online: Persistent B cell memory after SARS-CoV-2 vaccination is functional during breakthrough infections.

Terreri, Sara / Piano Mortari, Eva / Vinci, Maria Rosaria / Russo, Cristina / Alteri, Claudia / Albano, Christian / Colavita, Francesca / Gramigna, Giulia / Agrati, Chiara / Linardos, Giulia / Coltella, Luana / Colagrossi, Luna / Deriu, Gloria / Ciofi Degli Atti, Marta / Rizzo, Caterina / Scarsella, Marco / Brugaletta, Rita / Camisa, Vincenzo / Santoro, Annapaola /

Roscilli, Giuseppe / Pavoni, Emiliano / Muzi, Alessia / Magnavita, Nicola / Scutari, Rossana / Villani, Alberto / Raponi, Massimiliano / Locatelli, Franco / Perno, Carlo Federico / Zaffina, Salvatore / Carsetti, Rita

Cell host & microbe

2022 Volume 30, Issue 3, Page(s) 400–408.e4

Abstract: Breakthrough SARS-CoV-2 infections in fully vaccinated individuals are considered a consequence of waning immunity. Serum antibodies represent the most measurable outcome of vaccine-induced B cell memory. When antibodies decline, memory B cells are ... ...

Abstract	Breakthrough SARS-CoV-2 infections in fully vaccinated individuals are considered a consequence of waning immunity. Serum antibodies represent the most measurable outcome of vaccine-induced B cell memory. When antibodies decline, memory B cells are expected to persist and perform their function, preventing clinical disease. We investigated whether BNT162b2 mRNA vaccine induces durable and functional B cell memory in vivo against SARS-CoV-2 3, 6, and 9 months after the second dose in a cohort of health care workers (HCWs). While we observed physiological decline of SARS-CoV-2-specific antibodies, memory B cells persist and increase until 9 months after immunization. HCWs with breakthrough infections had no signs of waning immunity. In 3-4 days, memory B cells responded to SARS-CoV-2 infection by producing high levels of specific antibodies in the serum and anti-Spike IgA in the saliva. Antibodies to the viral nucleoprotein were produced with the slow kinetics typical of the response to a novel antigen.
MeSH term(s)	Antibodies, Viral ; BNT162 Vaccine ; COVID-19/prevention & control ; COVID-19 Vaccines ; Humans ; SARS-CoV-2 ; Vaccination ; Vaccines, Synthetic ; mRNA Vaccines
Chemical Substances	Antibodies, Viral ; COVID-19 Vaccines ; Vaccines, Synthetic ; mRNA Vaccines ; BNT162 Vaccine (N38TVC63NU)
Language	English
Publishing date	2022-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2022.01.003
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Article ; Online: Highly Specific Memory B Cells Generation after the 2nd Dose of BNT162b2 Vaccine Compensate for the Decline of Serum Antibodies and Absence of Mucosal IgA.

Piano Mortari, Eva / Russo, Cristina / Vinci, Maria Rosaria / Terreri, Sara / Fernandez Salinas, Ane / Piccioni, Livia / Alteri, Claudia / Colagrossi, Luna / Coltella, Luana / Ranno, Stefania / Linardos, Giulia / Agosta, Marilena / Albano, Christian / Agrati, Chiara / Castilletti, Concetta / Meschi, Silvia / Romania, Paolo / Roscilli, Giuseppe / Pavoni, Emiliano /

Camisa, Vincenzo / Santoro, Annapaola / Brugaletta, Rita / Magnavita, Nicola / Ruggiero, Alessandra / Cotugno, Nicola / Amodio, Donato / Ciofi Degli Atti, Marta Luisa / Giorgio, Daniela / Russo, Nicoletta / Salvatori, Guglielmo / Corsetti, Tiziana / Locatelli, Franco / Perno, Carlo Federico / Zaffina, Salvatore / Carsetti, Rita

Cells

2021 Volume 10, Issue 10

Abstract: Specific memory B cells and antibodies are a reliable read-out of vaccine efficacy. We analysed these biomarkers after one and two doses of BNT162b2 vaccine. The second dose significantly increases the level of highly specific memory B cells and ... ...

Abstract	Specific memory B cells and antibodies are a reliable read-out of vaccine efficacy. We analysed these biomarkers after one and two doses of BNT162b2 vaccine. The second dose significantly increases the level of highly specific memory B cells and antibodies. Two months after the second dose, specific antibody levels decline, but highly specific memory B cells continue to increase, thus predicting a sustained protection from COVID-19. We show that although mucosal IgA is not induced by the vaccination, memory B cells migrate in response to inflammation and secrete IgA at mucosal sites. We show that the first vaccine dose may lead to an insufficient number of highly specific memory B cells and low concentration of serum antibodies, thus leaving vaccinees without the immune robustness needed to ensure viral elimination and herd immunity. We also clarify that the reduction of serum antibodies does not diminish the force and duration of the immune protection induced by vaccination. The vaccine does not induce sterilizing immunity. Infection after vaccination may be caused by the lack of local preventive immunity because of the absence of mucosal IgA.
MeSH term(s)	Adult ; Antibodies, Neutralizing/blood ; Antibodies, Viral/immunology ; Antigens, Viral/immunology ; B-Lymphocytes/cytology ; B-Lymphocytes/immunology ; COVID-19/immunology ; COVID-19/prevention & control ; COVID-19 Vaccines/therapeutic use ; Cryopreservation ; Female ; Health Personnel ; Healthy Volunteers ; Hospitals, Pediatric ; Humans ; Immunoglobulin A/immunology ; Immunoglobulin G ; Immunoglobulin M/immunology ; Immunologic Memory ; Lactation ; Male ; Middle Aged ; Mucous Membrane/immunology ; Patient Safety ; SARS-CoV-2 ; Vaccination
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Antigens, Viral ; COVID-19 Vaccines ; Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M ; BNT162 vaccine (N38TVC63NU)
Language	English
Publishing date	2021-09-26
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10102541
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