Recombinant Antibodies to the Ebola Virus Glycoprotein

Панина, А. А.; Dementieva, I. G.; Алиев, Т. К.; Toporova, V. A.; Balabashin, D. S.; Bokov, M. N.; Pozdnyakova, L. P.; Shchemchukova, O. B.; Долгих, Д. А.; Свешников, П. Г.; Kirpichnikov, Mikhaǐl P.

doi:10.32607/20758251-2017-9-4-84-91

Cited by 4 publications

(1 citation statement)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…An analysis of the CI values allows one to infer that the epitopes of the full-length recombinant epitopes GPE118, GPE325, and GPE534, chimeric Fab fragments [ 13 ], and the parental murine mAbs coincide. All three candidate anti-EBOV GP antibodies are also targeted against different epitopes.…”

Section: Resultsmentioning

confidence: 99%

Recombinant Antibodies to the Ebola Virus Glycoprotein

Panina¹,

Dementieva²,

Aliev³

et al. 2018

Acta Naturae

Self Cite

View full text Add to dashboard Cite

Currently, there are no approved therapies for targeted prevention and treatment of Ebola hemorrhagic fever. In the present work, we describe the development of a eukaryotic expression system for the production of three full-length chimeric antibodies (IgG1-kappa isotypes) GPE118, GPE325, and GPE534 to the recombinant glycoprotein of the Ebola virus (EBOV GP), which is a key factor in the pathogenicity of the disease. The immunochemical properties of the obtained antibodies were studied by immunoblotting and indirect, direct, and competitive ELISA using the recombinant EBOV proteins rGPdTM, NP, and VP40. The authenticity of the antibodies and the absence of cross-specificity with respect to the structural proteins NP and VP40 of the Ebola virus were proved. The epitope specificity of the resulting recombinant antibodies was studied using commercial neutralizing antibodies against the viral glycoprotein. The recombinant antibodies GPE118, GPE325, and GPE534 were shown to recognize glycoprotein epitopes that coincide or overlap with the epitopes of three well-studied neutralizing anti-Ebola virus antibodies.

show abstract

Section: Resultsmentioning

confidence: 99%

Recombinant Antibodies to the Ebola Virus Glycoprotein

Panina¹,

Dementieva²,

Aliev³

et al. 2018

Acta Naturae

Self Cite

View full text Add to dashboard Cite

show abstract

Antibody affinity as a driver of signal generation in a paper-based immunoassay for Ebola virus surveillance

et al. 2021

View full text Add to dashboard Cite

Graphical abstract During epidemics, such as the frequent and devastating Ebola virus outbreaks that have historically plagued regions of Africa, serological surveillance efforts are critical for viral containment and the development of effective antiviral therapeutics. Antibody serology can also be used retrospectively for population-level surveillance to provide a more complete estimate of total infections. Ebola surveillance efforts rely on enzyme-linked immunosorbent assays (ELISAs), which restrict testing to laboratories and are not adaptable for use in resource-limited settings. In this manuscript, we describe a paper-based immunoassay capable of detecting anti-Ebola IgG using Ebola virus envelope glycoprotein ectodomain (GP) as the affinity reagent. We evaluated seven monoclonal antibodies (mAbs) against GP—KZ52, 13C6, 4G7, 2G4, c6D8, 13F6, and 4F3—to elucidate the impact of binding affinity and binding epitope on assay performance and, ultimately, result interpretation. We used biolayer interferometry to characterize the binding of each antibody to GP before assessing their performance in our paper-based device. Binding affinity (K D ) and on rate (k on ) were major factors influencing the sensitivity of the paper-based immunoassay. mAbs with the best K D (3–25 nM) exhibited the lowest limits of detection (ca. μg mL −1 ), while mAbs with K D > 25 nM were undetectable in our device. Additionally, and most surprisingly, we determined that observed signals in paper devices were directly proportional to k on . These results highlight the importance of ensuring that the quality of recognition reagents is sufficient to support desired assay performance and suggest that the strength of an individual’s immune response can impact the interpretation of assay results. Supplementary Information The online version contains supplementary material available at 10.1007/s00216-021-03317-4.

show abstract