scholarly journals Structural basis of tetanus toxin neutralization by native human monoclonal antibodies

Cell Reports ◽  
2021 ◽  
Vol 35 (5) ◽  
pp. 109070
Author(s):  
Yueming Wang ◽  
Changwen Wu ◽  
Jinfang Yu ◽  
Shujian Lin ◽  
Tong Liu ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Tetanus Toxin ◽  
Structural Basis ◽  
Human Monoclonal Antibodies

scholarly journals Structural basis for cooperativity of human monoclonal antibodies to meningococcal factor H-binding protein

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Ilaria Peschiera ◽  
Maria Giuliani ◽  
Fabiola Giusti ◽  
Roberto Melero ◽  
Eugenio Paccagnini ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Binding Protein ◽  
Factor H ◽  
Structural Basis ◽  
Human Monoclonal Antibodies

Establishment of hybridomas secreting human monoclonal antibodies against tetanus toxin and hepatitis B virus surface antigen

1985 ◽  
Vol 129 (1) ◽  
pp. 26-33 ◽  
Author(s):  
Yuzo Ichimori ◽  
Kazunori Sasano ◽  
Hiroko Itoh ◽  
Shinya Hitotsumachi ◽  
Yoshiaki Kimura ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Surface Antigen ◽  
Tetanus Toxin ◽  
Human Monoclonal Antibodies ◽  
Virus Surface ◽  
Virus Surface Antigen ◽  
B Virus

Protection of Mice Against Tetanus Toxin by Combination of Two Human Monoclonal Antibodies Recognizing Distinct Epitopes on the Toxin Molecule

Hybridoma ◽  
1986 ◽  
Vol 5 (1) ◽  
pp. 21-31 ◽  
Author(s):  
H.W. LÖMS ZIEGLER-HEITBROCK ◽  
CHRISTIAN REITER ◽  
JUTTA TRENKMANN ◽  
AGNES FÜTTERER ◽  
GERT RIETHMÜLLER
Keyword(s):  
Monoclonal Antibodies ◽  
Tetanus Toxin ◽  
Human Monoclonal Antibodies ◽  
Toxin Molecule

Human monoclonal antibodies with a protective activity against tetanus toxin

Apmis ◽  
1989 ◽  
Vol 97 (7-12) ◽  
pp. 671-676 ◽  
Author(s):  
M.-A. TRABAUD ◽  
L. LERY ◽  
C. DESGRANGES
Keyword(s):  
Monoclonal Antibodies ◽  
Tetanus Toxin ◽  
Protective Activity ◽  
Human Monoclonal Antibodies

scholarly journals Structural Basis of HCV Neutralization by Human Monoclonal Antibodies Resistant to Viral Neutralization Escape

2013 ◽  
Vol 9 (5) ◽  
pp. e1003364 ◽  
Author(s):  
Thomas Krey ◽  
Annalisa Meola ◽  
Zhen-yong Keck ◽  
Laurence Damier-Piolle ◽  
Steven K. H. Foung ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Structural Basis ◽  
Human Monoclonal Antibodies ◽  
Viral Neutralization

Neutralization of Tetanus Toxin by Human Monoclonal Antibodies Directed Against Tetanus Toxin Fragment C

Hybridoma ◽  
1993 ◽  
Vol 12 (6) ◽  
pp. 699-708 ◽  
Author(s):  
B. GUSTAFSSON ◽  
E. WHITMORE ◽  
M. TIRU
Keyword(s):  
Monoclonal Antibodies ◽  
Tetanus Toxin ◽  
Human Monoclonal Antibodies

scholarly journals An oligoclonal combination of human monoclonal antibodies able to neutralize tetanus toxin in vivo

Toxicon X ◽  
2019 ◽  
Vol 2 ◽  
pp. 100006 ◽  
Author(s):  
Eduardo Aliprandini ◽  
Daniela Yumi Takata ◽  
Ana Lepique ◽  
Jorge Kalil ◽  
Silvia Beatriz Boscardin ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Tetanus Toxin ◽  
Human Monoclonal Antibodies

scholarly journals Cryo-EM structures elucidate neutralizing mechanisms of anti-chikungunya human monoclonal antibodies with therapeutic activity

2015 ◽  
Vol 112 (45) ◽  
pp. 13898-13903 ◽  
Author(s):  
Feng Long ◽  
Rachel H. Fong ◽  
Stephen K. Austin ◽  
Zhenguo Chen ◽  
Thomas Klose ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Chikungunya Virus ◽  
Structural Basis ◽  
Binding Studies ◽  
Viral Glycoprotein ◽  
Human Monoclonal Antibodies ◽  
Human Mabs ◽  
Alanine Scanning Mutagenesis ◽  
Viral Surface ◽  
Fusion Loop

Chikungunya virus (CHIKV) is a mosquito-transmitted alphavirus that causes severe acute and chronic disease in humans. Although highly inhibitory murine and human monoclonal antibodies (mAbs) have been generated, the structural basis of their neutralizing activity remains poorly characterized. Here, we determined the cryo-EM structures of chikungunya virus-like particles complexed with antibody fragments (Fab) of two highly protective human mAbs, 4J21 and 5M16, that block virus fusion with host membranes. Both mAbs bind primarily to sites within the A and B domains, as well as to the B domain’s β-ribbon connector of the viral glycoprotein E2. The footprints of these antibodies on the viral surface were consistent with results from loss-of-binding studies using an alanine scanning mutagenesis-based epitope mapping approach. The Fab fragments stabilized the position of the B domain relative to the virus, particularly for the complex with 5M16. This finding is consistent with a mechanism of neutralization in which anti-CHIKV mAbs that bridge the A and B domains impede movement of the B domain away from the underlying fusion loop on the E1 glycoprotein and therefore block the requisite pH-dependent fusion of viral and host membranes.

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