Epitopes of Naturally Acquired and Vaccine-Induced Anti-Ebola Virus Glycoprotein Antibodies in Single Amino Acid Resolution
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Epitopes of Naturally Acquired and Vaccine-Induced Anti-Ebola Virus Glycoprotein Antibodies in Single Amino Acid Resolution. / Heidepriem, Jasmin; Krähling, Verena; Dahlke, Christine; Wolf, Timo; Klein, Florian; Addo, Marylyn M; Becker, Stephan; Loeffler, Felix F.
In: BIOTECHNOL J, Vol. 15, No. 9, 09.2020, p. e2000069.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Epitopes of Naturally Acquired and Vaccine-Induced Anti-Ebola Virus Glycoprotein Antibodies in Single Amino Acid Resolution
AU - Heidepriem, Jasmin
AU - Krähling, Verena
AU - Dahlke, Christine
AU - Wolf, Timo
AU - Klein, Florian
AU - Addo, Marylyn M
AU - Becker, Stephan
AU - Loeffler, Felix F
N1 - © 2020 The Authors. Biotechnology Journal published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2020/9
Y1 - 2020/9
N2 - The Ebola virus (EBOV) can cause severe infections in humans, leading to a fatal outcome in a high percentage of cases. Neutralizing antibodies against the EBOV surface glycoprotein (GP) can prevent infections, demonstrating a straightforward way for an efficient vaccination strategy. Meanwhile, many different anti-EBOV antibodies have been identified, whereas the exact binding epitopes are often unknown. Here, the analysis of serum samples from an EBOV vaccine trial with the recombinant vesicular stomatitis virus-Zaire ebolavirus (rVSV-ZEBOV) and an Ebola virus disease survivor, using high-density peptide arrays, is presented. In this proof-of-principle study, distinct IgG and IgM antibodies binding to different epitopes of EBOV GP is detected: By mapping the whole GP as overlapping peptide fragments, new epitopes and confirmed epitopes from the literature are found. Furthermore, the highly selective binding epitope of a neutralizing monoclonal anti-EBOV GP antibody could be validated. This shows that peptide arrays can be a valuable tool to study the humoral immune response to vaccines in patients and to support Ebola vaccine development.
AB - The Ebola virus (EBOV) can cause severe infections in humans, leading to a fatal outcome in a high percentage of cases. Neutralizing antibodies against the EBOV surface glycoprotein (GP) can prevent infections, demonstrating a straightforward way for an efficient vaccination strategy. Meanwhile, many different anti-EBOV antibodies have been identified, whereas the exact binding epitopes are often unknown. Here, the analysis of serum samples from an EBOV vaccine trial with the recombinant vesicular stomatitis virus-Zaire ebolavirus (rVSV-ZEBOV) and an Ebola virus disease survivor, using high-density peptide arrays, is presented. In this proof-of-principle study, distinct IgG and IgM antibodies binding to different epitopes of EBOV GP is detected: By mapping the whole GP as overlapping peptide fragments, new epitopes and confirmed epitopes from the literature are found. Furthermore, the highly selective binding epitope of a neutralizing monoclonal anti-EBOV GP antibody could be validated. This shows that peptide arrays can be a valuable tool to study the humoral immune response to vaccines in patients and to support Ebola vaccine development.
U2 - 10.1002/biot.202000069
DO - 10.1002/biot.202000069
M3 - SCORING: Journal article
C2 - 32463974
VL - 15
SP - e2000069
JO - BIOTECHNOL J
JF - BIOTECHNOL J
SN - 1860-6768
IS - 9
ER -
