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Your search keyword '"Balistreri, Giuseppe"' showing total 3 results
Start Over Author "Balistreri, Giuseppe" Publisher american association for the advancement of science
3 results on '"Balistreri, Giuseppe"'

1. Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity

Author

Cantuti-Castelvetri, Ludovico; https://orcid.org/0000-0002-0642-1610, Ojha, Ravi; https://orcid.org/0000-0001-7876-4607, Pedro, Liliana D; https://orcid.org/0000-0003-3556-647X, Djannatian, Minou; https://orcid.org/0000-0002-7759-6557, Franz, Jonas; https://orcid.org/0000-0001-7523-6622, Kuivanen, Suvi; https://orcid.org/0000-0002-2347-5397, van der Meer, Franziska; https://orcid.org/0000-0002-9433-9173, Kallio, Katri, Kaya, Tuğberk; https://orcid.org/0000-0001-5926-8608, Anastasina, Maria; https://orcid.org/0000-0002-4555-6446, Smura, Teemu, Levanov, Lev, Szirovicza, Leonora; https://orcid.org/0000-0003-1528-044X, Tobi, Allan; https://orcid.org/0000-0003-4797-5481, Kallio-Kokko, Hannimari, Österlund, Pamela; https://orcid.org/0000-0002-2229-6661, Joensuu, Merja; https://orcid.org/0000-0002-4533-0455, Meunier, Frédéric A; https://orcid.org/0000-0001-6400-1107, Butcher, Sarah J; https://orcid.org/0000-0001-7060-5871, Winkler, Martin Sebastian, Mollenhauer, Brit, Helenius, Ari, Gokce, Ozgun; https://orcid.org/0000-0001-6319-404X, Teesalu, Tambet; https://orcid.org/0000-0002-9458-6385, Hepojoki, Jussi; https://orcid.org/0000-0001-5699-214X, Vapalahti, Olli; https://orcid.org/0000-0003-2270-6824, Stadelmann, Christine; https://orcid.org/0000-0003-1766-5458, Balistreri, Giuseppe; https://orcid.org/0000-0002-3585-559X, Simons, Mikael; https://orcid.org/0000-0001-5329-192X, Cantuti-Castelvetri, Ludovico; https://orcid.org/0000-0002-0642-1610, Ojha, Ravi; https://orcid.org/0000-0001-7876-4607, Pedro, Liliana D; https://orcid.org/0000-0003-3556-647X, Djannatian, Minou; https://orcid.org/0000-0002-7759-6557, Franz, Jonas; https://orcid.org/0000-0001-7523-6622, Kuivanen, Suvi; https://orcid.org/0000-0002-2347-5397, van der Meer, Franziska; https://orcid.org/0000-0002-9433-9173, Kallio, Katri, Kaya, Tuğberk; https://orcid.org/0000-0001-5926-8608, Anastasina, Maria; https://orcid.org/0000-0002-4555-6446, Smura, Teemu, Levanov, Lev, Szirovicza, Leonora; https://orcid.org/0000-0003-1528-044X, Tobi, Allan; https://orcid.org/0000-0003-4797-5481, Kallio-Kokko, Hannimari, Österlund, Pamela; https://orcid.org/0000-0002-2229-6661, Joensuu, Merja; https://orcid.org/0000-0002-4533-0455, Meunier, Frédéric A; https://orcid.org/0000-0001-6400-1107, Butcher, Sarah J; https://orcid.org/0000-0001-7060-5871, Winkler, Martin Sebastian, Mollenhauer, Brit, Helenius, Ari, Gokce, Ozgun; https://orcid.org/0000-0001-6319-404X, Teesalu, Tambet; https://orcid.org/0000-0002-9458-6385, Hepojoki, Jussi; https://orcid.org/0000-0001-5699-214X, Vapalahti, Olli; https://orcid.org/0000-0003-2270-6824, Stadelmann, Christine; https://orcid.org/0000-0003-1766-5458, Balistreri, Giuseppe; https://orcid.org/0000-0002-3585-559X, and Simons, Mikael; https://orcid.org/0000-0001-5329-192X

Abstract

The causative agent of coronavirus disease 2019 (COVID-19) is the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). For many viruses, tissue tropism is determined by the availability of virus receptors and entry cofactors on the surface of host cells. In this study, we found that neuropilin-1 (NRP1), known to bind furin-cleaved substrates, significantly potentiates SARS-CoV-2 infectivity, an effect blocked by a monoclonal blocking antibody against NRP1. A SARS-CoV-2 mutant with an altered furin cleavage site did not depend on NRP1 for infectivity. Pathological analysis of olfactory epithelium obtained from human COVID-19 autopsies revealed that SARS-CoV-2 infected NRP1-positive cells facing the nasal cavity. Our data provide insight into SARS-CoV-2 cell infectivity and define a potential target for antiviral intervention.

Published
2020

2. SARS-CoV-2 infection and viral fusogens cause neuronal and glial fusion that compromises neuronal activity.

Author

Martínez-Mármol, Ramón, Giordano-Santini, Rosina, Kaulich, Eva, Ann-Na Cho, Przybyla, Magdalena, Riyadh, Md Asrafuzzaman, Robinson, Emilija, Keng Yih Chew, Amor, Rumelo, Meunier, Frédéric A., Balistreri, Giuseppe, Short, Kirsty R., Ke, Yazi D., Ittner, Lars M., and Hilliard, Massimo A.

Subjects
*SARS-CoV-2, *VIRUS diseases
Abstract

The article discusses effect of structural and computational design severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and viral fusogens on neuronal activity. It mentions that SARS-CoV-2 infection induces fusion between neurons and glia in mouse and human brain organoids, where it mentions that neuronal fusion is a progressive and can lead to the formation of multicellular syncytia which further compromises neuronal activity.

Published
2023
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3. Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.

Author

Cantuti-Castelvetri L, Ojha R, Pedro LD, Djannatian M, Franz J, Kuivanen S, van der Meer F, Kallio K, Kaya T, Anastasina M, Smura T, Levanov L, Szirovicza L, Tobi A, Kallio-Kokko H, Österlund P, Joensuu M, Meunier FA, Butcher SJ, Winkler MS, Mollenhauer B, Helenius A, Gokce O, Teesalu T, Hepojoki J, Vapalahti O, Stadelmann C, Balistreri G, and Simons M

Subjects
Angiotensin-Converting Enzyme 2, Animals, Antibodies, Monoclonal immunology, Betacoronavirus genetics, COVID-19, Caco-2 Cells, Female, HEK293 Cells, Host Microbial Interactions, Humans, Lung metabolism, Male, Metal Nanoparticles, Mice, Mice, Inbred C57BL, Mutation, Neuropilin-1 chemistry, Neuropilin-1 genetics, Neuropilin-1 immunology, Neuropilin-2 metabolism, Olfactory Mucosa metabolism, Olfactory Mucosa virology, Pandemics, Peptide Fragments metabolism, Peptidyl-Dipeptidase A genetics, Peptidyl-Dipeptidase A metabolism, Protein Binding, Protein Domains, Respiratory Mucosa metabolism, SARS-CoV-2, Serine Endopeptidases genetics, Serine Endopeptidases metabolism, Spike Glycoprotein, Coronavirus chemistry, Betacoronavirus physiology, Coronavirus Infections virology, Neuropilin-1 metabolism, Pneumonia, Viral virology, Spike Glycoprotein, Coronavirus metabolism, Virus Internalization
Abstract

The causative agent of coronavirus disease 2019 (COVID-19) is the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). For many viruses, tissue tropism is determined by the availability of virus receptors and entry cofactors on the surface of host cells. In this study, we found that neuropilin-1 (NRP1), known to bind furin-cleaved substrates, significantly potentiates SARS-CoV-2 infectivity, an effect blocked by a monoclonal blocking antibody against NRP1. A SARS-CoV-2 mutant with an altered furin cleavage site did not depend on NRP1 for infectivity. Pathological analysis of olfactory epithelium obtained from human COVID-19 autopsies revealed that SARS-CoV-2 infected NRP1-positive cells facing the nasal cavity. Our data provide insight into SARS-CoV-2 cell infectivity and define a potential target for antiviral intervention., (Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)

Published
2020
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