scholarly journals Purification and characterization of monoclonal IgG antibodies recognizing Ebola virus glycoprotein

2018 ◽  
Vol 7 (2) ◽  
pp. 119 ◽  
Author(s):  
Baek-Sang Han ◽  
Ho-Young Jang ◽  
Trina Racine ◽  
Xiangguo Qiu ◽  
Jeong-Im Sin
Keyword(s):  
Ebola Virus ◽  
Igg Antibodies ◽  
Purification And Characterization ◽  
Virus Glycoprotein

scholarly journals Characterization of the inhibitory effect of an extract of Prunella vulgaris on Ebola virus glycoprotein (GP)-mediated virus entry and infection

2016 ◽  
Vol 127 ◽  
pp. 20-31 ◽  
Author(s):  
Xu Zhang ◽  
Zhujun Ao ◽  
Alexander Bello ◽  
Xiaozhuo Ran ◽  
Shuiping Liu ◽  
...  
Keyword(s):  
Ebola Virus ◽  
Virus Entry ◽  
Inhibitory Effect ◽  
Prunella Vulgaris ◽  
Virus Glycoprotein

scholarly journals Development and characterization of monoclonal antibodies to Ebola virus glycoprotein

2016 ◽  
Vol 71 (1) ◽  
pp. 24-28 ◽  
Author(s):  
O. B. Schemchukova ◽  
I. G. Dement’yeva ◽  
N. E. Varlamov ◽  
L. P. Pozdnyakova ◽  
M. N. Bokov ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Ebola Virus ◽  
Virus Glycoprotein

Transient and stable CHO expression, purification and characterization of novel hetero-dimeric bispecific IgG antibodies

2017 ◽  
Vol 33 (2) ◽  
pp. 469-477 ◽  
Author(s):  
Yashas Rajendra ◽  
Robert B. Peery ◽  
Maria D. Hougland ◽  
Gavin C. Barnard ◽  
Xiufeng Wu ◽  
...  
Keyword(s):  
Igg Antibodies ◽  
Purification And Characterization

Characterization of oligomerization of a peptide from the ebola virus glycoprotein by small-angle neutron scattering

2016 ◽  
Vol 61 (1) ◽  
pp. 94-97
Author(s):  
V. V. Egorov ◽  
A. N. Gorshkov ◽  
T. N. Murugova ◽  
A. V. Vasin ◽  
D. V. Lebedev ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Ebola Virus ◽  
Virus Glycoprotein

scholarly journals Further characterization of the immune response in mice to inactivated and live rabies vaccines expressing Ebola virus glycoprotein

Vaccine ◽  
2012 ◽  
Vol 30 (43) ◽  
pp. 6136-6141 ◽  
Author(s):  
Amy B. Papaneri ◽  
Christoph Wirblich ◽  
Kurt Cooper ◽  
Peter B. Jahrling ◽  
Matthias J. Schnell ◽  
...  
Keyword(s):  
Immune Response ◽  
Ebola Virus ◽  
Virus Glycoprotein

scholarly journals Affinity-Purified Human Immunoglobulin G That Binds a Lacto-N-Neotetraose-Dependent Lipooligosaccharide Structure Is Bactericidal for Serogroup B Neisseria meningitidis

2006 ◽  
Vol 75 (2) ◽  
pp. 1025-1033 ◽  
Author(s):  
Michele M. Estabrook ◽  
Gary A. Jarvis ◽  
J. McLeod Griffiss
Keyword(s):  
Immunoglobulin G ◽  
Enzyme Linked Immunosorbent Assay ◽  
Igg Antibodies ◽  
Purification And Characterization ◽  
Technological Advances ◽  
Specific Igg ◽  
Bactericidal Activities ◽  
Group B ◽  
Disseminated Disease

ABSTRACT Despite technological advances, no vaccine to prevent serogroup B meningococcal disease is available. The failure to develop a vaccine has shifted the focus to an alternative outer membrane structure, lipooligosaccharide (LOS), because disseminated disease induces bactericidal immunoglobulin G (IgG) that binds LOS. The purpose of this study was to identify the LOS structure(s) that induces human bactericidal IgG by purification and characterization of these antibodies. Human LOS IgG antibodies were affinity purified by passage of intravenous immunoglobulin through purified, type-specific LOS having a known structure coupled to epoxy-activated Sepharose 6B. Pathogenic group B strains representing the major LOS serotypes were used to examine the binding and bactericidal activities of four LOS-specific IgG preparations. All four LOS-specific IgG preparations bound to strains expressing homologous, as well as heterologous, LOS serotypes as determined by flow cytometry and an enzyme-linked immunosorbent assay. With human complement, IgG that was purified with L7 LOS was bactericidal for strains expressing L3,7 and L2,4 LOS, serotypes expressed by the majority of disease-associated group B and C meningococci. In conclusion, we purified human LOS-specific IgG that binds meningococci across LOS glycose-specific serotypes. An antigen that is dependent on the glycose lacto-N-neotetraose induces IgG in humans that is bactericidal for L2, L3, L4, and L7 strains. A vaccine containing this antigen would have the potential to protect against the vast majority of group B meningococcal strains.

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