scholarly journals Identification and Structural Characterization of a Broadly Neutralizing Antibody Targeting a Novel Conserved Epitope on the Influenza Virus H5N1 Hemagglutinin

2012 ◽  
Vol 87 (4) ◽  
pp. 2215-2225 ◽  
Author(s):  
L. Du ◽  
L. Jin ◽  
G. Zhao ◽  
S. Sun ◽  
J. Li ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Structural Characterization ◽  
Neutralizing Antibody ◽  
Virus H5n1 ◽  
Broadly Neutralizing Antibody ◽  
Antibody Targeting ◽  
Conserved Epitope

scholarly journals Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Christopher O. Barnes ◽  
Harry B. Gristick ◽  
Natalia T. Freund ◽  
Amelia Escolano ◽  
Artem Y. Lyubimov ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Neutralizing Antibody ◽  
Broadly Neutralizing Antibody ◽  
Hiv 1

scholarly journals A broadly neutralizing antibody protects against SARS-CoV, pre-emergent bat CoVs, and SARS-CoV-2 variants in mice

2021 ◽  
Author(s):  
David R. Martinez ◽  
Alexandra Schaefer ◽  
Sophie Gobeil ◽  
Dapeng Li ◽  
Gabriela De la Cruz ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Receptor Binding ◽  
Specific Antibody ◽  
Neutralizing Antibody ◽  
Affinity Binding ◽  
Receptor Binding Domain ◽  
High Affinity Binding ◽  
High Affinity ◽  
Broadly Neutralizing Antibody ◽  
Conserved Epitope

AbstractSARS-CoV in 2003, SARS-CoV-2 in 2019, and SARS-CoV-2 variants of concern (VOC) can cause deadly infections, underlining the importance of developing broadly effective countermeasures against Group 2B Sarbecoviruses, which could be key in the rapid prevention and mitigation of future zoonotic events. Here, we demonstrate the neutralization of SARS-CoV, bat CoVs WIV-1 and RsSHC014, and SARS-CoV-2 variants D614G, B.1.1.7, B.1.429, B1.351 by a receptor-binding domain (RBD)-specific antibody DH1047. Prophylactic and therapeutic treatment with DH1047 demonstrated protection against SARS-CoV, WIV-1, RsSHC014, and SARS-CoV-2 B1.351infection in mice. Binding and structural analysis showed high affinity binding of DH1047 to an epitope that is highly conserved among Sarbecoviruses. We conclude that DH1047 is a broadly neutralizing and protective antibody that can prevent infection and mitigate outbreaks caused by SARS-like strains and SARS-CoV-2 variants. Our results argue that the RBD conserved epitope bound by DH1047 is a rational target for pan Group 2B coronavirus vaccines.

scholarly journals Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus

2010 ◽  
Vol 6 (8) ◽  
pp. e1001034 ◽  
Author(s):  
Shinya Yamada ◽  
Masato Hatta ◽  
Bart L. Staker ◽  
Shinji Watanabe ◽  
Masaki Imai ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Structural Characterization

Selection and characterization of DNA aptamers for use in detection of avian influenza virus H5N1

2013 ◽  
Vol 189 (2) ◽  
pp. 362-369 ◽  
Author(s):  
Ronghui Wang ◽  
Jingjing Zhao ◽  
Tieshan Jiang ◽  
Young M. Kwon ◽  
Huaguang Lu ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Dna Aptamers ◽  
Virus H5n1 ◽  
Avian Influenza Virus H5n1

scholarly journals Characterization of broadly neutralizing antibody responses to HIV-1 in a cohort of long term non-progressors

PLoS ONE ◽  
2018 ◽  
Vol 13 (3) ◽  
pp. e0193773 ◽  
Author(s):  
Nuria González ◽  
Krisha McKee ◽  
Rebecca M. Lynch ◽  
Ivelin S. Georgiev ◽  
Laura Jimenez ◽  
...  
Keyword(s):  
Neutralizing Antibody ◽  
Antibody Responses ◽  
Broadly Neutralizing Antibody ◽  
Hiv 1

D108 Synthetic HIV-1 Glycopeptides Enable Characterization of Fine Epitopes of Broadly Neutralizing Antibody PG9

2013 ◽  
Vol 62 ◽  
pp. S50
Author(s):  
Mohammed N. Amin ◽  
Jason S. McLellan ◽  
Wei Huang ◽  
Jared Orwenyo ◽  
Peter D. Kwong ◽  
...  
Keyword(s):  
Neutralizing Antibody ◽  
Broadly Neutralizing Antibody ◽  
Hiv 1

Characterization of an avian influenza virus H5N1 Egyptian isolate

2009 ◽  
Vol 159 (2) ◽  
pp. 244-250 ◽  
Author(s):  
M.M. Bahgat ◽  
M.A. Kutkat ◽  
M.H. Nasraa ◽  
A. Mostafa ◽  
R. Webby ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Virus H5n1 ◽  
Avian Influenza Virus H5n1 ◽  
Egyptian Isolate

scholarly journals Comparing Antigenicity and Immunogenicity of Engineered gp120

2005 ◽  
Vol 79 (19) ◽  
pp. 12148-12163 ◽  
Author(s):  
Suganya Selvarajah ◽  
Bridget Puffer ◽  
Ralph Pantophlet ◽  
Mansun Law ◽  
Robert W. Doms ◽  
...  
Keyword(s):  
Neutralizing Antibodies ◽  
Neutralizing Antibody ◽  
Significant Degree ◽  
Wild Type ◽  
Cd4 Binding Site ◽  
Monomeric Gp120 ◽  
Broadly Neutralizing Antibody ◽  
The Relationship ◽  
Conserved Epitope ◽  
Better Than

ABSTRACT We have engineered monomeric gp120 in such a way as to favorably present the conserved epitope for the broadly neutralizing antibody b12 while lowering the exposure of epitopes recognized by some weakly neutralizing and nonneutralizing antibodies. The work presented here describes the immune response in rabbits immunized with two prototype, engineered gp120s to explore the relationship between antigenicity and immunogenicity for these mutants. The GDMR gp120 mutant (residues 473 to 476 on gp120 altered from GDMR to AAAA) has a series of substitutions on the edge of the CD4 binding site (CD4bs), and the mCHO gp120 mutant has seven extra glycans relative to the wild-type protein. Importantly, serum mapping showed that both mutants did not elicit antibodies against a number of epitopes that had been targeted for dampening. The sera from rabbits immunized with the GDMR gp120 mutant neutralized some primary viruses at levels somewhat better than the wild-type gp120 immune sera as a result of an increased elicitation of anti-V3 antibodies. Unlike wild-type gp120 immune sera, GDMR gp120 immune sera failed to neutralize HXBc2, a T-cell line adapted (TCLA) virus. This was associated with loss of CD4bs/CD4-induced antibodies that neutralize TCLA but not primary viruses. The mCHO gp120 immune sera did not neutralize primary viruses to any significant degree, reflecting the masking of epitopes of even weakly neutralizing antibodies without eliciting b12-like antibodies. These results show that antibody responses to multiple epitopes on gp120 can be dampened. More precise focusing to a neutralizing epitope will likely require several iterations comparing antigenicity and immunogenicity of engineered proteins.

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