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Everardo R. Rodríguez-Rodríguez
Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, UNAM, Apartado Postal 510-3, Cuernavaca, Morelos 62250, Mexico

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Journal article
Published: 10 January 2019 in Toxins
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The recombinant antibody fragments generated against the toxic components of scorpion venoms are considered a promising alternative for obtaining new antivenoms for therapy. Using directed evolution and site-directed mutagenesis, it was possible to generate a human single-chain antibody fragment with a broad cross-reactivity that retained recognition for its original antigen. This variant is the first antibody fragment that neutralizes the effect of an estimated 13 neurotoxins present in the venom of nine species of Mexican scorpions. This single antibody fragment showed the properties of a polyvalent antivenom. These results represent a significant advance in the development of new antivenoms against scorpion stings, since the number of components would be minimized due to their broad cross-neutralization capacity, while at the same time bypassing animal immunization.

ACS Style

Lidia Riaño-Umbarila; Ilse V. Gómez-Ramírez; Luis M. Ledezma-Candanoza; Timoteo Olamendi-Portugal; Everardo Remi Rodríguez-Rodríguez; Guillermo Fernández-Taboada; Lourival D. Possani; Baltazar Becerril. Generation of a Broadly Cross-Neutralizing Antibody Fragment against Several Mexican Scorpion Venoms. Toxins 2019, 11, 32 .

AMA Style

Lidia Riaño-Umbarila, Ilse V. Gómez-Ramírez, Luis M. Ledezma-Candanoza, Timoteo Olamendi-Portugal, Everardo Remi Rodríguez-Rodríguez, Guillermo Fernández-Taboada, Lourival D. Possani, Baltazar Becerril. Generation of a Broadly Cross-Neutralizing Antibody Fragment against Several Mexican Scorpion Venoms. Toxins. 2019; 11 (1):32.

Chicago/Turabian Style

Lidia Riaño-Umbarila; Ilse V. Gómez-Ramírez; Luis M. Ledezma-Candanoza; Timoteo Olamendi-Portugal; Everardo Remi Rodríguez-Rodríguez; Guillermo Fernández-Taboada; Lourival D. Possani; Baltazar Becerril. 2019. "Generation of a Broadly Cross-Neutralizing Antibody Fragment against Several Mexican Scorpion Venoms." Toxins 11, no. 1: 32.

Journal article
Published: 01 November 2017 in Toxicon
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The increment in the number of scorpion envenoming cases in Mexico is mainly associated to the rapid growth of the urban areas, and consequently, to the invasion of natural habitats of these arachnids. On the other hand, there is a great diversity of scorpion species, so it is indispensable to identify those of medical importance, which we now know are many more than the 7-8 previously reported as dangerous to humans. Because different LD50 values have been reported for the venom of the same species, probably due to variations in the experimental conditions used, in this work we determined the LD50 values for the venoms of 13 different species of scorpions using simple but systematic procedures. This information constitutes a referent on the level of toxicity of medically important scorpion species from Mexico and establishes the bases for a more comprehensive assessment of the neutralizing capacity of current and developing antivenoms.

ACS Style

Lidia Riaño-Umbarila; Everardo R. Rodríguez-Rodríguez; Carlos E. Santibañez-López; Leopoldo Güereca; Selene J. Uribe-Romero; Ilse V. Gómez-Ramírez; Edson N. Cárcamo-Noriega; Lourival D. Possani; Baltazar Becerril. Updating knowledge on new medically important scorpion species in Mexico. Toxicon 2017, 138, 130 -137.

AMA Style

Lidia Riaño-Umbarila, Everardo R. Rodríguez-Rodríguez, Carlos E. Santibañez-López, Leopoldo Güereca, Selene J. Uribe-Romero, Ilse V. Gómez-Ramírez, Edson N. Cárcamo-Noriega, Lourival D. Possani, Baltazar Becerril. Updating knowledge on new medically important scorpion species in Mexico. Toxicon. 2017; 138 ():130-137.

Chicago/Turabian Style

Lidia Riaño-Umbarila; Everardo R. Rodríguez-Rodríguez; Carlos E. Santibañez-López; Leopoldo Güereca; Selene J. Uribe-Romero; Ilse V. Gómez-Ramírez; Edson N. Cárcamo-Noriega; Lourival D. Possani; Baltazar Becerril. 2017. "Updating knowledge on new medically important scorpion species in Mexico." Toxicon 138, no. : 130-137.

Journal article
Published: 01 September 2016 in Toxicon
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New approaches aimed at neutralizing the primary toxic components present in scorpion venoms, represent a promising alternative to the use of antivenoms of equine origin in humans. New potential therapeutics developed by these approaches correspond to neutralizing antibody fragments obtained by selection and maturation processes from libraries of human origin. The high sequence identity shared among scorpion toxins is associated with an important level of cross reactivity exhibited by these antibody fragments. We have exploited the cross reactivity showed by single chain variable antibody fragments (scFvs) of human origin to re-direct the neutralizing capacity toward various other scorpion toxins. As expected, during these evolving processes several variants derived from a parental scFv exhibited the capacity to simultaneously recognize and neutralize different toxins from Centruroides scorpion venoms. A sequence analyses of the cross reacting scFvs revealed that specific mutations are responsible for broadening their neutralizing capacity. In this work, we generated a set of new scFvs that resulted from the combinatorial insertion of these point mutations. These scFvs are potential candidates to be part of a novel recombinant antivenom of human origin that could confer protection against scorpion stings. A remarkable property of one of these new scFvs (ER-5) is its capacity to neutralize at least three different toxins and its complementary capacity to neutralize the whole venom from Centruroides suffusus in combination with a second scFv (LR), which binds to a different epitope shared by Centruroides scorpion toxins.

ACS Style

Everardo Rodríguez; Timoteo Olamendi-Portugal; Hugo Serrano-Posada; Jonathan Noé Arredondo-López; Ilse Gómez-Ramírez; Guillermo Fernández-Taboada; Lourival D. Possani; Gerardo Alfonso Anguiano-Vega; Lidia Riaño-Umbarila; Baltazar Becerril. Broadening the neutralizing capacity of a family of antibody fragments against different toxins from Mexican scorpions. Toxicon 2016, 119, 52 -63.

AMA Style

Everardo Rodríguez, Timoteo Olamendi-Portugal, Hugo Serrano-Posada, Jonathan Noé Arredondo-López, Ilse Gómez-Ramírez, Guillermo Fernández-Taboada, Lourival D. Possani, Gerardo Alfonso Anguiano-Vega, Lidia Riaño-Umbarila, Baltazar Becerril. Broadening the neutralizing capacity of a family of antibody fragments against different toxins from Mexican scorpions. Toxicon. 2016; 119 ():52-63.

Chicago/Turabian Style

Everardo Rodríguez; Timoteo Olamendi-Portugal; Hugo Serrano-Posada; Jonathan Noé Arredondo-López; Ilse Gómez-Ramírez; Guillermo Fernández-Taboada; Lourival D. Possani; Gerardo Alfonso Anguiano-Vega; Lidia Riaño-Umbarila; Baltazar Becerril. 2016. "Broadening the neutralizing capacity of a family of antibody fragments against different toxins from Mexican scorpions." Toxicon 119, no. : 52-63.

Book chapter
Published: 24 December 2014 in Scorpion Venoms
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The detailed knowledge of the medically important components within the venoms from poisonous animals has prompted the rational generation of improved antivenoms. The new generation of antivenoms, in the case of scorpion envenoming, will be based on the neutralization of the toxins directed against mammalian ion channels, specifically sodium channels. The neutralization of the major toxic molecules declines the lethality of the whole venom. The next generation of antivenoms will depend substantially on the advancements in the field of antibody engineering. The accumulation of detailed information of antibody structure and function proposes that human recombinant antibodies in combination with phage display and directed evolution as a powerful in vitro biotechnological platform alternative to classical antivenoms or monoclonal antibodies for the generation of outstanding therapeutic antibodies. This biotechnological platform has allowed the isolation of safe and efficient recombinant neutralizing antibodies. Many antibody fragments generated using this platform bear exceptional properties that had not been reached using classical approaches. This review describes the great progress that has been achieved on the improvement of antivenoms against scorpion envenoming which have been generated using the already mentioned platform as compared with classical and/or hybridoma approaches.

ACS Style

Everardo Remi Rodríguez Rodríguez; Lidia Riaño Umbarila; Lourival D. Possani; Baltazar Becerril. Recombinant Neutralizing Antibodies, A New Generation of Antivenoms. Scorpion Venoms 2014, 139 -159.

AMA Style

Everardo Remi Rodríguez Rodríguez, Lidia Riaño Umbarila, Lourival D. Possani, Baltazar Becerril. Recombinant Neutralizing Antibodies, A New Generation of Antivenoms. Scorpion Venoms. 2014; ():139-159.

Chicago/Turabian Style

Everardo Remi Rodríguez Rodríguez; Lidia Riaño Umbarila; Lourival D. Possani; Baltazar Becerril. 2014. "Recombinant Neutralizing Antibodies, A New Generation of Antivenoms." Scorpion Venoms , no. : 139-159.

Book chapter
Published: 01 January 2013 in Toxins and Drug Discovery
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The detailed knowledge of the medically important components within the venoms from poisonous animals has prompted the rational generation of improved antivenoms. The new generation of antivenoms, in the case of scorpion envenoming, will be based on the neutralization of the toxins directed against mammalian ion channels, specifically sodium channels. The neutralization of the major toxic molecules declines the lethality of the whole venom. The next generation of antivenoms will depend substantially on the advancements in the field of antibody engineering. The accumulation of detailed information of antibody structure and function proposes that human recombinant antibodies in combination with phage display and directed evolution as a powerful in vitro biotechnological platform alternative to classical antivenoms or monoclonal antibodies for the generation of outstanding therapeutic antibodies. This biotechnological platform has allowed the isolation of safety and efficient recombinant neutralizing antibodies. Many antibody fragments generated using this platform bear exceptional properties that had not been reached using classical approaches. This review describes the great progress that has been achieved on the improvement of antivenoms against scorpion envenoming which have been generated using the already mentioned platform as compared with classical and/or hybridoma approaches.

ACS Style

Everardo Remi Rodríguez Rodríguez; Lidia Riaño Umbarila; Lourival D. Possani; Dr. Baltazar Becerril. Recombinant Neutralizing Antibodies, A New Generation of Antivenoms. Toxins and Drug Discovery 2013, 1 -19.

AMA Style

Everardo Remi Rodríguez Rodríguez, Lidia Riaño Umbarila, Lourival D. Possani, Dr. Baltazar Becerril. Recombinant Neutralizing Antibodies, A New Generation of Antivenoms. Toxins and Drug Discovery. 2013; ():1-19.

Chicago/Turabian Style

Everardo Remi Rodríguez Rodríguez; Lidia Riaño Umbarila; Lourival D. Possani; Dr. Baltazar Becerril. 2013. "Recombinant Neutralizing Antibodies, A New Generation of Antivenoms." Toxins and Drug Discovery , no. : 1-19.

Journal article
Published: 01 October 2012 in Journal of Molecular Biology
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Excellent results regarding improved therapeutic properties have been often obtained through the conversion of a single-chain variable fragment (scFv) into a noncovalent dimeric antibody (diabody) via peptide linker shortening. We utilized this approach to obtain a dimeric version of the human scFv 6009F, which was originally engineered to neutralize the Cn2 toxin of Centruroides noxius scorpion venom. However, some envenoming symptoms remained with diabody 6009F. Diabody 6009F was subjected to directed evolution to obtain a variant capable of eliminating envenoming symptoms. After two rounds of biopanning, diabody D4 was isolated. It exhibited a single mutation (E43G) in framework 2 of the heavy-chain variable domain. Diabody D4 displayed an increase in T(m) (thermal transition midpoint temperature) of 6.3°C compared with its dimeric precursor. The importance of the E43G mutation was tested in the context of the human scFv LR, a highly efficient antibody against Cn2, which was previously generated by our group [Riaño-Umbarila, L., Contreras-Ferrat, G., Olamendi-Portugal, T., Morelos-Juárez, C., Corzo, G., Possani, L. D. and Becerril, B. (2011). J. Biol. Chem.286, 6143-6151]. The new variant, scFv LER, displayed an increase in T(m) of 3.4°C and was capable of neutralizing 2 LD(50) of Cn2 toxin with no detectable symptoms when injected into mice at a 1:1 toxin-to-antibody molar ratio. These results showed that the E43G mutation might increase the therapeutic properties of these antibody fragments. Molecular modeling and dynamics results suggest that the rearrangement of the hydrogen-bonding network near the E43G mutation could explain the improved functional stability and neutralization properties of both the diabody D4 and scFv LER.

ACS Style

Everardo Remi Rodríguez-Rodríguez; Luis M. Ledezma-Candanoza; Luis Gabriel Contreras-Ferrat; Timoteo Olamendi-Portugal; Lourival D. Possani; Baltazar Becerril; Lidia Riaño-Umbarila. A Single Mutation in Framework 2 of the Heavy Variable Domain Improves the Properties of a Diabody and a Related Single-Chain Antibody. Journal of Molecular Biology 2012, 423, 337 -350.

AMA Style

Everardo Remi Rodríguez-Rodríguez, Luis M. Ledezma-Candanoza, Luis Gabriel Contreras-Ferrat, Timoteo Olamendi-Portugal, Lourival D. Possani, Baltazar Becerril, Lidia Riaño-Umbarila. A Single Mutation in Framework 2 of the Heavy Variable Domain Improves the Properties of a Diabody and a Related Single-Chain Antibody. Journal of Molecular Biology. 2012; 423 (3):337-350.

Chicago/Turabian Style

Everardo Remi Rodríguez-Rodríguez; Luis M. Ledezma-Candanoza; Luis Gabriel Contreras-Ferrat; Timoteo Olamendi-Portugal; Lourival D. Possani; Baltazar Becerril; Lidia Riaño-Umbarila. 2012. "A Single Mutation in Framework 2 of the Heavy Variable Domain Improves the Properties of a Diabody and a Related Single-Chain Antibody." Journal of Molecular Biology 423, no. 3: 337-350.