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30 results on '"Almagro, Juan Carlos"'

2. Antibody Engineering & Therapeutics, The Annual Meeting of The Antibody Society: December 8-12, 2013, Huntington Beach, CA

Author

Almagro, Juan Carlos, Gilliland, Gary L, Breden, Felix, Scott, Jamie K, Sok, Devin, Pauthner, Matthias, Reichert, Janice M, Helguera, Gustavo, Andrabi, Raiees, Mabry, Robert, Bléry, Mathieu, Voss, James E, Laurén, Juha, Abuqayyas, Lubna, Barghorn, Stefan, Ben-Jacob, Eshel, Crowe, James E, Jr, Huston, James S, Johnston, Stephen Albert, Krauland, Eric, Lund-Johansen, Fridtjof, Marasco, Wayne A, Parren, Paul WHI, and Xu, Kai Y

Published
2014

3. Development and Evaluation of a Set of Spike and Receptor Binding Domain-Based Enzyme-Linked Immunosorbent Assays for SARS-CoV-2 Serological Testing

Author

Camacho-Sandoval, Rosa, primary, Nieto-Patlán, Alejandro, additional, Carballo-Uicab, Gregorio, additional, Montes-Luna, Alejandra, additional, Jiménez-Martínez, María C., additional, Vallejo-Castillo, Luis, additional, González-González, Edith, additional, Arrieta-Oliva, Hugo Iván, additional, Gómez-Castellano, Keyla, additional, Guzmán-Bringas, Omar U., additional, Cruz-Domínguez, María Pilar, additional, Medina, Gabriela, additional, Montiel-Cervantes, Laura A., additional, Gordillo-Marín, Maricela, additional, Vázquez-Campuzano, Roberto, additional, Torres-Longoria, Belem, additional, López-Martínez, Irma, additional, Pérez-Tapia, Sonia M., additional, and Almagro, Juan Carlos, additional

Published
2021
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7. Isolation and characterization of high affinity and highly stable anti-Chikungunya virus antibodies using ALTHEA Gold Libraries™

Author

Pedraza-Escalona, Martha, primary, Guzmán-Bringas, Omar, additional, Arrieta-Oliva, Ivan, additional, Gómez-Castellano, Keyla, additional, Salinas-Trujano, Juana, additional, Torres-Flores, Jesus, additional, Muñoz-Herrera, Juan, additional, Camacho-Sandoval, Rosa, additional, Contreras-Pineda, Paola, additional, Chacón-Salinas, Rommel, additional, Pérez-Tapia, Sonia Mayra, additional, and Almagro, Juan Carlos, additional

Published
2020
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12. Structural insights into humanization of anti-tissue factor antibody 10H10

Author

Teplyakov, Alexey, primary, Obmolova, Galina, additional, Malia, Thomas J., additional, Raghunathan, Gopalan, additional, Martinez, Christian, additional, Fransson, Johan, additional, Edwards, Wilson, additional, Connor, Judith, additional, Husovsky, Matthew, additional, Beck, Heena, additional, Chi, Ellen, additional, Fenton, Sandra, additional, Zhou, Hong, additional, Almagro, Juan Carlos, additional, and Gilliland, Gary L., additional

Published
2018
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15. Antibody modeling assessment II. Structures and models

Author

Teplyakov, Alexey, primary, Luo, Jinquan, additional, Obmolova, Galina, additional, Malia, Thomas J., additional, Sweet, Raymond, additional, Stanfield, Robyn L., additional, Kodangattil, Sreekumar, additional, Almagro, Juan Carlos, additional, and Gilliland, Gary L., additional

Published
2014
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16. Antibody Engineering and Therapeutics

Author

Almagro, Juan Carlos, primary, Gilliland, Gary L, additional, Breden, Felix, additional, Scott, Jamie K, additional, Sok, Devin, additional, Pauthner, Matthias, additional, Reichert, Janice M, additional, Helguera, Gustavo, additional, Andrabi, Raiees, additional, Mabry, Robert, additional, Bléry, Mathieu, additional, Voss, James E, additional, Laurén, Juha, additional, Abuqayyas, Lubna, additional, Barghorn, Stefan, additional, Ben-Jacob, Eshel, additional, Crowe, James E, additional, Huston, James S, additional, Johnston, Stephen Albert, additional, Krauland, Eric, additional, Lund-Johansen, Fridtjof, additional, Marasco, Wayne A, additional, Parren, Paul WHI, additional, and Xu, Kai Y, additional

Published
2014
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18. Characterization of a high-affinity human antibody with a disulfide bridge in the third complementarity-determining region of the heavy chain

Author

Almagro, Juan Carlos, primary, Raghunathan, Gopalan, additional, Beil, Eric, additional, Janecki, Dariusz J., additional, Chen, Qiang, additional, Dinh, Thai, additional, LaCombe, Ann, additional, Connor, Judy, additional, Ware, Mark, additional, Kim, Paul H., additional, Swanson, Ronald V., additional, and Fransson, Johan, additional

Published
2012
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26. Corrigendum

Author

Vargas-Madrazo, Enrique, primary, Lara-Ochoa, Francisco, additional, and Almagro, Juan Carlos, additional

Published
1996
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28. Design and validation of a synthetic VH repertoire with tailored diversity for protein recognition.

Author

Almagro, Juan Carlos, Quintero-Hernández, Veronica, Ortiz-León, Mauricio, Velandia, Alvaro, Smith, Sylvia L., and Becerril, Baltazar

Abstract

Previous studies have indicated differences in the specificity-determining residues (SDRs) of antibodies that recognize haptens, peptides, or proteins. Here, we designed a VH repertoire based on the human scaffold 3-23/JH4 and diversification of high and medium-usage SDRs of anti-protein and anti-peptide antibodies. The repertoire was synthesized by overlapping polymerase chain reaction (PCR) and combined with the VL chain of the anti-hen egg-white lysozyme (HEL) antibody D1.3. The resulting chimeric single-chain Fv fragments (scFvs) phage-displayed library was panned in HEL-coated immunotubes. After two rounds of selection under non-stringent conditions, that is, trypsinization after 2 h of incubation at room temperature, 63 of 167 clones analyzed (38%) were found to express scFvs specific to HEL. Twenty clones were characterized by DNA sequencing resulting in 10 unique scFvs. Interestingly, the panel of unique scFvs was highly diverse, with VH sequences differing in 16 of the 17 positions variegated in the repertoire. Thus, diverse chemico-physical and structural solutions were selected from the library, even when the VH repertoire was constrained by the VL chain of D1.3 to yield binders against a definite region of HEL surface. The more often selected scFvs, namely H6-1 and B7-1, which differed in eight SDRs, showed levels of expression in E. coli TG1 strain, 6 and 10 times higher than the parental D1.3 Fv fragment, respectively. Dissociation constants ( KDs) measured in the BIAcore were 11 and 6.6 nM for H6-1 and B7-1, respectively. These values compared well to the KD of 4.7 nM measured for D1.3, indicating that the VH repertoire here designed is a valuable source of diverse, well-expressed and high affinity VH domains. Copyright © 2006 John Wiley & Sons, Ltd. [ABSTRACT FROM AUTHOR]

Published
2006
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29. Canonical Structure Repertoire of the Antigen-binding Site of Immunoglobulins Suggests Strong Geometrical Restrictions Associated to the Mechanism of Immune Recognition

Author

Vargas-Madrazo, Enrique, Lara-Ochoa, Francisco, and Almagro, Juan Carlos

Abstract

Is the structural repertoire of immunoglobulins free to adopt an almost infinite number of conformations to build the diversity of the immune response or does it take advantage of only a few conformations? In this paper we study this question by applying the canonical structure model to characterize the structural repertoire of immunoglobulins. The results found, indicate that only ten combinations out of the 300 possible different canonical structure classes (combinations of canonical structures), make up 87% of 381 sequences analyzed. This suggests that the structural repertoire of immunoglobulins is restricted to the preferential use of a small number of canonical structure classes. The possible functional significance of these results was studied by analyzing the correspondence between the observed canonical structural repertoire implicit in Ig sequences and the types of antigens recognized. Two different sets of canonical structure classes were distinguished: one with preference for some specific types of antigens like proteins, polysaccharides or haptens, and the other with multi-specific binding capabilities. Analysis of antibodies of known three-dimensional structure shows that for two specific classes, the canonical conformations of H2 and L1 determine the geometrical characteristics of the antigen-binding site, while at least in one multi-specific class, the changes in the general geometry of the antigen-binding site are produced by different conformations of H3. Implications of these results for the molecular recognition process mediated by immunoglobulins are discussed.

Published
1995
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30. Leveraging SBDD in protein therapeutic development: antibody engineering.

Author

Gilliland GL, Luo J, Vafa O, and Almagro JC

Subjects
Antibodies chemistry, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Structure, Antibodies therapeutic use, Drug Design, Protein Engineering
Abstract

Antibodies make up the largest, growing segment of protein therapeutics in the pharmaceutical and biotechnology industries. The development or engineering of therapeutic antibodies is based to a large extent on our knowledge of antibody structure and requires sophisticated methods that continue to evolve. In this chapter, after a review of what is known about the structure and functional properties of antibodies, the current, state-of-the-art antibody engineering methods are described. These methods include antibody humanization, antigen-affinity optimization, Fc engineering for modulated effector function and extended half-life, and engineering for improved stability and biophysical properties. X-ray crystallographic structures of antibody fragments and their complexes can play a critical role in guiding and, in some cases, accelerating these processes. These approaches represent guidelines for developing antibody therapeutics with the desired affinity, effector function, and biophysical properties.

Published
2012
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