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Camelid VHHs Fused to Human Fc Fragments Provide Long Term Protection Against Botulinum Neurotoxin A in Mice

by Solovyev, Andrey I. , Esmagambetov, Ilias B. , Noskov, Anatoly N. , Ugriumova, Galina A. , Logunov, Denis Y. , Godakova, Svetlana A. , Tukhvatulin, Amir I. , Shcheblyakov, Dmitry V. , Vinogradova, Irina D. , Naroditsky, Boris S. , Gintsburg, Aleksandr L.

in Antibodies / Antigens / Antitoxins / Binding sites / Blood / Blood circulation / Botulinum toxin type A / Botulism / camelid single-domain antibodies / Cloning / Clostridium botulinum / Complementarity-determining region 3 / dimers / Display devices / Fatalities / Fc fragments / Food contamination / Food contamination & poisoning / IgG antibody / Immunization / Immunoglobulin G / Intoxication / Lethal dose / Microorganisms / Nanobodies / Nervous system / Neurotoxins / Neutralizing / Phage display / Phages / toxin neutralization / Toxins / VHH

2019

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Camelid VHHs Fused to Human Fc Fragments Provide Long Term Protection Against Botulinum Neurotoxin A in Mice

2019

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Camelid VHHs Fused to Human Fc Fragments Provide Long Term Protection Against Botulinum Neurotoxin A in Mice

2019

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Journal Article

Camelid VHHs Fused to Human Fc Fragments Provide Long Term Protection Against Botulinum Neurotoxin A in Mice

Solovyev, Andrey I.,

Esmagambetov, Ilias B.,

Noskov, Anatoly N.,

Ugriumova, Galina A.,

Logunov, Denis Y.,

Godakova, Svetlana A.,

Tukhvatulin, Amir I.,

Shcheblyakov, Dmitry V.,

Vinogradova, Irina D.,

Naroditsky, Boris S.,

Gintsburg, Aleksandr L.

2019

Overview

The bacterium Clostridium botulinum is the causative agent of botulism—a severe intoxication caused by botulinum neurotoxin (BoNT) and characterized by damage to the nervous system. In an effort to develop novel C. botulinum immunotherapeutics, camelid single-domain antibodies (sdAbs, VHHs, or nanobodies) could be used due to their unique structure and characteristics. In this study, VHHs were produced using phage display technology. A total of 15 different monoclonal VHHs were selected based on their comlementarity-determining region 3 (CDR3) sequences. Different toxin lethal dose (LD50) challenges with each selected phage clone were conducted in vivo to check their neutralizing potency. We demonstrated that modification of neutralizing VHHs with a human immunoglobulin G (IgG)1 Fc (fragment crystallizable) fragment (fusionbody, VHH-Fc) significantly increased the circulation time in the blood (up to 14 days). At the same time, VHH-Fc showed the protective activity 1000 times higher than monomeric form when challenged with 5 LD50. Moreover, VHH-Fcs remained protective even 14 days after antibody administration. These results indicate that this VHH-Fc could be used as an effective long term antitoxin protection against botulinum type A.

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Publisher

MDPI AG,MDPI

Subject

/ Blood

/ Botulinum toxin type A