scholarly journals Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein

2020 ◽  
Author(s):  
Antoni Wrobel ◽  
Donald Benton ◽  
Saira Hussain ◽  
Ruth Harvey ◽  
Chloë Roustan ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Antibody Binding ◽  
Spike Glycoprotein

Abstract The CR3022 antibody, selected from a group of SARS-CoV-1 monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using electron cryo-microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.

scholarly journals Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Antoni G. Wrobel ◽  
Donald J. Benton ◽  
Saira Hussain ◽  
Ruth Harvey ◽  
Stephen R. Martin ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibodies ◽  
Antibody Binding ◽  
Spike Glycoprotein ◽  
Cryo Electron Microscopy

Abstract The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.

scholarly journals Identification of Novel Neutralizing Monoclonal Antibodies against SARS-CoV-2 Spike Glycoprotein

2021 ◽  
Author(s):  
Devivasha Bordoloi ◽  
Ziyang Xu ◽  
Michelle Ho ◽  
Mansi Purwar ◽  
Pratik Bhojnagarwala ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Spike Glycoprotein

scholarly journals Mechanisms of Allergen-Antibody Interaction of Cockroach Allergen Bla g 2 with Monoclonal Antibodies That Inhibit IgE Antibody Binding

PLoS ONE ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. e22223 ◽  
Author(s):  
Jill Glesner ◽  
Sabina Wünschmann ◽  
Mi Li ◽  
Alla Gustchina ◽  
Alexander Wlodawer ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Antibody Binding ◽  
Ige Antibody ◽  
Cockroach Allergen

scholarly journals Multiple Tolerization Reduces Antibody Binding Against Tolerogen Cells: Implications for the Production of Monoclonal Antibodies

2018 ◽  
Vol 37 (2) ◽  
pp. 100-104
Author(s):  
Rodrigo de Almeida ◽  
Cecília Naomi Nakamura ◽  
Marina de Lima Fontes ◽  
Julia Paiola da Silva ◽  
Matheus Bertanha ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Antibody Binding

Identification and characterization of monoclonal antibodies that partially block human natural antibody binding to pig endothelial cell xenoantigens

1996 ◽  
Vol 3 (4) ◽  
pp. 287-295 ◽  
Author(s):  
Mary Kearns-Jonker ◽  
Donald V. Cramer ◽  
Mark Fraiman ◽  
Yvette Middleton ◽  
Amal Shirwan ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Endothelial Cell ◽  
Antibody Binding ◽  
Natural Antibody ◽  
Identification And Characterization

scholarly journals Identification of osteoclast-specific monoclonal antibodies.

1985 ◽  
Vol 100 (5) ◽  
pp. 1592-1600 ◽  
Author(s):  
M J Oursler ◽  
L V Bell ◽  
B Clevinger ◽  
P Osdoby
Keyword(s):  
Monoclonal Antibodies ◽  
Giant Cells ◽  
Mononuclear Phagocyte ◽  
Antibody Binding ◽  
Enzyme Linked Immunosorbent Assay ◽  
Form And Function ◽  
Titration Curves ◽  
Specific Antigens ◽  
And Function

Studies on the origin, identification, and characterization of osteoclasts have been difficult. This is in part due to a lack of definitive osteoclast markers and the similarity of these cells in form and function to cells of the mononuclear phagocyte system. To solve this problem, we inoculated isolated chick osteoclasts into mice to generate osteoclast-specific monoclonal antibodies. Supernatants from growth-positive hybridomas were screened by indirect immunofluorescent methods against cultured osteoclasts, monocyte-derived multinucleated giant cells, cultured monocytes, fibroblasts, and limb mesenchyme. Select hybridomas were cloned to produce 375 clones, which were analyzed as described above. Antibody from select clones was also reacted with paraffin sections of bone. In addition, two clones have been analyzed by enzyme-linked immunosorbent assay (ELISA) and Western blot analysis. Antibody binding from an osteoclast-specific clone and a clone reactive with osteoclasts, giant cells, and cultured monocytes (as determined by immunohistochemical assay) was confirmed by antibody-binding and titration curves quantitated by ELISA. The above studies demonstrate that osteoclast specific antigens exist, and that osteoclasts, giant cells, and cultured monocytes share common determinants not found on other cells screened.

scholarly journals High-Resolution Mapping of Human Norovirus Antigens via Genomic Phage Display Library Selections and Deep Sequencing

2020 ◽  
Vol 95 (1) ◽  
Author(s):  
Wanzhi Huang ◽  
Victoria Soeung ◽  
David M. Boragine ◽  
Liya Hu ◽  
B. V. Venkataram Prasad ◽  
...  
Keyword(s):  
Immune Response ◽  
Monoclonal Antibodies ◽  
Deep Sequencing ◽  
Binding Sites ◽  
Neutralizing Antibodies ◽  
Phage Display Library ◽  
Antibody Binding ◽  
Affinity Selection ◽  
Humoral Immune ◽  
Polyclonal Antisera

ABSTRACT Norovirus (NoV) infections are a leading cause of gastroenteritis. The humoral immune response plays an important role in the control of NoV, and recent studies have identified neutralizing antibodies that bind the capsid protein VP1 to block viral infection. Here, we utilize a NoV GI.1 Jun-Fos-assisted phage display library constructed from randomly fragmented genomic DNA coupled with affinity selection for antibody binding and subsequent deep sequencing to map epitopes. The epitopes were identified by quantitating the phage clones before and after affinity selection and aligning the sequences of the most enriched peptides. The HJT-R3-A9 single-chain variable fragment (scFv) antibody epitope was mapped to a 12-amino-acid region of VP1 that is also the binding site for several previously identified monoclonal antibodies. We synthesized the 12-mer peptide and found that it binds the scFv antibody with a KD (equilibrium dissociation constant) of 46 nM. Further, alignment of enriched peptides after affinity selection on rabbit anti-NoV polyclonal antisera revealed five families of overlapping sequences that define distinct epitopes in VP1. One of these is identical to the HJT-R3-A9 scFv epitope, further suggesting that it is immunodominant. Similarly, other epitopes identified using the polyclonal antisera overlap binding sites for previously reported monoclonal antibodies, suggesting that they are also dominant epitopes. The results demonstrate that affinity selection and deep sequencing of the phage library provide sufficient resolution to map multiple epitopes simultaneously from complex samples such as polyclonal antisera. This approach can be extended to examine the antigenic landscape in patient sera to facilitate investigation of the immune response to NoV. IMPORTANCE NoV infections are a leading cause of gastroenteritis in the United States. Human NoVs exhibit extensive genetic and antigenic diversity, which makes it challenging to design a vaccine that provides broad protection against infection. Antibodies developed during the immune response play an important role in the control of NoV infections. Neutralizing antibodies that act by sterically blocking the site on the virus used to bind human cells have been identified. Identification of other antibody binding sites associated with virus neutralization is therefore of interest. Here, we use a high-resolution method to map multiple antibody binding sites simultaneously from complex serum samples. The results show that a relatively small number of sites on the virus bind a large number of independently generated antibodies, suggesting that immunodominance plays a role in the humoral immune response to NoV infections.

scholarly journals Towards a solution to MERS: protective human monoclonal antibodies targeting different domains and functions of the MERS-coronavirus spike glycoprotein

2019 ◽  
Vol 8 (1) ◽  
pp. 516-530 ◽  
Author(s):  
Ivy Widjaja ◽  
Chunyan Wang ◽  
Rien van Haperen ◽  
Javier Gutiérrez-Álvarez ◽  
Brenda van Dieren ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Spike Glycoprotein ◽  
Human Monoclonal Antibodies
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