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Your search keyword '"Doranz, Benjamin J."' showing total 22 results
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22 results on '"Doranz, Benjamin J."'

1. Targeting the Spike Receptor Binding Domain Class V Cryptic Epitope by an Antibody with Pan-Sarbecovirus Activity

Author

Jensen, Jaime L., primary, Sankhala, Rajeshwer S., additional, Dussupt, Vincent, additional, Bai, Hongjun, additional, Hajduczki, Agnes, additional, Lal, Kerri G., additional, Chang, William C., additional, Martinez, Elizabeth J., additional, Peterson, Caroline E., additional, Golub, Emily S., additional, Rees, Phyllis A., additional, Mendez-Rivera, Letzibeth, additional, Zemil, Michelle, additional, Kavusak, Erin, additional, Mayer, Sandra V., additional, Wieczorek, Lindsay, additional, Kannan, Shruthi, additional, Doranz, Benjamin J., additional, Davidson, Edgar, additional, Yang, Eun Sung, additional, Zhang, Yi, additional, Chen, Man, additional, Choe, Misook, additional, Wang, Lingshu, additional, Gromowski, Gregory D., additional, Koup, Richard A., additional, Michael, Nelson L., additional, Polonis, Victoria R., additional, Rolland, Morgane, additional, Modjarrad, Kayvon, additional, Krebs, Shelly J., additional, and Joyce, M. Gordon, additional

Published
2023
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2. Somatic Hypermutation and Framework Mutations of Variable Region Contribute to Anti-Zika Virus-Specific Monoclonal Antibody Binding and Function

Author

Tsuji, Isamu, primary, Vang, Fue, additional, Dominguez, David, additional, Karwal, Lovkesh, additional, Sanjali, Ankita, additional, Livengood, Jill A., additional, Davidson, Edgar, additional, Fouch, Mallorie E., additional, Doranz, Benjamin J., additional, Das, Subash C., additional, and Dean, Hansi J., additional

Published
2022
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3. A Novel Antigenic Site Spanning Domains I and III of the Zika Virus Envelope Glycoprotein Is the Target of Strongly Neutralizing Human Monoclonal Antibodies

Author

Graham, Stephen D., primary, Tu, Huy A., additional, McElvany, Benjamin D., additional, Graham, Nancy R., additional, Grinyo, Ariadna, additional, Davidson, Edgar, additional, Doranz, Benjamin J., additional, Diehl, Sean A., additional, de Silva, Aravinda M., additional, and Markmann, Alena Janda, additional

Published
2021
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6. Early Human B Cell Response to Ebola Virus in Four U.S. Survivors of Infection

Author

Williamson, Lauren E., primary, Flyak, Andrew I., additional, Kose, Nurgun, additional, Bombardi, Robin, additional, Branchizio, Andre, additional, Reddy, Srikar, additional, Davidson, Edgar, additional, Doranz, Benjamin J., additional, Fusco, Marnie L., additional, Saphire, Erica O., additional, Halfmann, Peter J., additional, Kawaoka, Yoshihiro, additional, Piper, Ashley E., additional, Glass, Pamela J., additional, and Crowe, James E., additional

Published
2019
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8. Mapping the Human Memory B Cell and Serum Neutralizing Antibody Responses to Dengue Virus Serotype 4 Infection and Vaccination

Author

Nivarthi, Usha K., primary, Kose, Nurgun, additional, Sapparapu, Gopal, additional, Widman, Douglas, additional, Gallichotte, Emily, additional, Pfaff, Jennifer M., additional, Doranz, Benjamin J., additional, Weiskopf, Daniela, additional, Sette, Alessandro, additional, Durbin, Anna P., additional, Whitehead, Steve S., additional, Baric, Ralph, additional, Crowe, James E., additional, and de Silva, Aravinda M., additional

Published
2017
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10. Functional Transplant of a Dengue Virus Serotype 3 (DENV3)-Specific Human Monoclonal Antibody Epitope into DENV1

Author

Messer, William B., primary, Yount, Boyd L., additional, Royal, Scott R., additional, de Alwis, Ruklanthi, additional, Widman, Douglas G., additional, Smith, Scott A., additional, Crowe, James E., additional, Pfaff, Jennifer M., additional, Kahle, Kristen M., additional, Doranz, Benjamin J., additional, Ibarra, Kristie D., additional, Harris, Eva, additional, de Silva, Aravinda M., additional, and Baric, Ralph S., additional

Published
2016
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11. Dengue Virus prM-Specific Human Monoclonal Antibodies with Virus Replication-Enhancing Properties Recognize a Single Immunodominant Antigenic Site

Author

Smith, Scott A., primary, Nivarthi, Usha K., additional, de Alwis, Ruklanthi, additional, Kose, Nurgun, additional, Sapparapu, Gopal, additional, Bombardi, Robin, additional, Kahle, Kristen M., additional, Pfaff, Jennifer M., additional, Lieberman, Sherri, additional, Doranz, Benjamin J., additional, de Silva, Aravinda M., additional, and Crowe, James E., additional

Published
2016
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13. Exposure of Epitope Residues on the Outer Face of the Chikungunya Virus Envelope Trimer Determines Antibody Neutralizing Efficacy

Author

Fong, Rachel H., primary, Banik, Soma S. R., additional, Mattia, Kimberly, additional, Barnes, Trevor, additional, Tucker, David, additional, Liss, Nathan, additional, Lu, Kai, additional, Selvarajah, Suganya, additional, Srinivasan, Surabhi, additional, Mabila, Manu, additional, Miller, Adam, additional, Muench, Marcus O., additional, Michault, Alain, additional, Rucker, Joseph B., additional, Paes, Cheryl, additional, Simmons, Graham, additional, Kahle, Kristen M., additional, and Doranz, Benjamin J., additional

Published
2014
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15. Functional Analysis of Antibodies against Dengue Virus Type 4 Reveals Strain-Dependent Epitope Exposure That Impacts Neutralization and Protection

Author

Sukupolvi-Petty, Soila, primary, Brien, James D., additional, Austin, S. Kyle, additional, Shrestha, Bimmi, additional, Swayne, Sherri, additional, Kahle, Kristen, additional, Doranz, Benjamin J., additional, Johnson, Syd, additional, Pierson, Theodore C., additional, Fremont, Daved H., additional, and Diamond, Michael S., additional

Published
2013
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16. Mechanistic Study of Broadly Neutralizing Human Monoclonal Antibodies against Dengue Virus That Target the Fusion Loop

Author

Costin, Joshua M., primary, Zaitseva, Elena, additional, Kahle, Kristen M., additional, Nicholson, Cindo O., additional, Rowe, Dawne K., additional, Graham, Amanda S., additional, Bazzone, Lindsey E., additional, Hogancamp, Greg, additional, Figueroa Sierra, Marielys, additional, Fong, Rachel H., additional, Yang, Sung-Tae, additional, Lin, Li, additional, Robinson, James E., additional, Doranz, Benjamin J., additional, Chernomordik, Leonid V., additional, Michael, Scott F., additional, Schieffelin, John S., additional, and Isern, Sharon, additional

Published
2013
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19. Influence of theCCR2-V64IPolymorphism on Human Immunodeficiency Virus Type 1 Coreceptor Activity and on Chemokine Receptor Function of CCR2b, CCR3, CCR5, and CXCR4

Author

Lee, Benhur, primary, Doranz, Benjamin J., additional, Rana, Shalini, additional, Yi, Yanji, additional, Mellado, Mario, additional, Frade, Jose M. R., additional, Martinez-A., Carlos, additional, O’Brien, Stephen J., additional, Dean, Michael, additional, Collman, Ronald G., additional, and Doms, Robert W., additional

Published
1998
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20. Somatic Hypermutation and Framework Mutations of Variable Region Contribute to Anti-Zika Virus-Specific Monoclonal Antibody Binding and Function.

Author

Isamu Tsuji, Fue Vang, Dominguez, David, Karwal, Lovkesh, Ankita Sanjali, Livengood, Jill A., Davidson, Edgar, Fouch, Mallorie E., Doranz, Benjamin J., Das, Subash C., and Dean, Hansi J.

Subjects
*MONOCLONAL antibodies, *ZIKA virus infections, *PROTEIN precursors, *PROTEIN domains, *MEMBRANE proteins, *VIRUS-like particles
Abstract

Zika virus (ZIKV) is a global public health concern due to its ability to cause congenital Zika syndrome and lack of approved vaccine, therapeutic, or other control measures. We discovered eight novel rabbit monoclonal antibodies (MAbs) that bind to distinct ZIKV envelope protein epitopes. The majority of the MAbs were ZIKV specific and targeted the lateral ridge of the envelope (E) protein domain III, while the MAb with the highest neutralizing activity recognized a putative quaternary epitope spanning E protein domains I and III. One of the non-neutralizing MAbs specifically recognized ZIKV precursor membrane protein (prM). Somatic hypermutation of immunoglobulin variable regions increases antibody affinity maturation and triggers antibody class switching. Negative correlations were observed between the somatic hypermutation rate of the immunoglobulin heavy-chain variable region and antibody binding parameters such as equilibrium dissociation constant, dissociation constant, and half-maximal effective concentration value of MAb binding to ZIKV virus-like particles. Complementarity-determining regions recognize the antigen epitopes and are scaffolded by canonical framework regions. Reversion of framework region amino acids to the rabbit germ line sequence decreased anti-ZIKV MAb binding activity of some MAbs. Thus, antibody affinity maturation, including somatic hypermutation and framework region mutations, contributed to the binding and function of these anti-ZIKV MAbs. IMPORTANCE ZIKV is a global health concern against which no vaccine or therapeutics are available. We characterized eight novel rabbit monoclonal antibodies recognizing ZIKV envelope and prM proteins and studied the relationship between somatic hypermutation of complementarity-determining regions, framework regions, mutations, antibody specificity, binding, and neutralizing activity. The results contribute to understanding structural features and somatic mutation pathways by which potent Zika virus-neutralizing antibodies can evolve, including the role of antibody framework regions. [ABSTRACT FROM AUTHOR]

Published
2022
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21. Protective Capacity of the Human Anamnestic Antibody Response during Acute Dengue Virus Infection.

Author

Meihui Xu, Züst, Roland, Ying Xiu Toh, Pfaff, Jennifer M., Kahle, Kristen M., Davidson, Edgar, Doranz, Benjamin J., Velumani, Sumathy, Tukijan, Farhana, Cheng-I Wang, and Fink, Katja

Subjects
*DENGUE, *IMMUNE response, *MONOCLONAL antibodies, *GLYCOPROTEINS, *STATISTICAL correlation, *VACCINATION
Abstract

Half of the world's population is exposed to the risk of dengue virus infection. Although a vaccine for dengue virus is now available in a few countries, its reported overall efficacy of about 60% is not ideal. Protective immune correlates following natural dengue virus infection remain undefined, which makes it difficult to predict the efficacy of new vaccines. In this study, we address the protective capacity of dengue virus-specific antibodies that are produced by plasmablasts a few days after natural secondary infection. Among a panel of 18 dengue virus-reactive human monoclonal antibodies, four groups of antibodies were identified based on their binding properties. While antibodies targeting the fusion loop of the glycoprotein of dengue virus dominated the antibody response, two smaller groups of antibodies bound to previously undescribed epitopes in domain II of the E protein. The latter, largely serotype-cross-reactive antibodies, demonstrated increased stability of binding at pH 5. These antibodies possessed weak to moderate neutralization capacity in vitro but were the most efficacious in promoting the survival of infected mice. Our data suggest that the cross-reactive anamnestic antibody response has a protective capacity despite moderate neutralization in vitro and a moderate decrease of viremia in vivo. [ABSTRACT FROM AUTHOR]

Published
2016
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22. Dengue Virus prM-Specific Human Monoclonal Antibodies with Virus Replication-Enhancing Properties Recognize a Single Immunodominant Antigenic Site.

Author

Smith SA, Nivarthi UK, de Alwis R, Kose N, Sapparapu G, Bombardi R, Kahle KM, Pfaff JM, Lieberman S, Doranz BJ, de Silva AM, and Crowe JE Jr

Subjects
Dengue Virus physiology, Epitope Mapping, Humans, Protein Binding, Antibodies, Monoclonal metabolism, Antibodies, Viral metabolism, Antibody-Dependent Enhancement, Dengue Virus drug effects, Epitopes metabolism, Viral Envelope Proteins metabolism, Virus Replication drug effects
Abstract

Unlabelled: The proposed antibody-dependent enhancement (ADE) mechanism for severe dengue virus (DENV) disease suggests that non-neutralizing serotype cross-reactive antibodies generated during a primary infection facilitate entry into Fc receptor bearing cells during secondary infection, resulting in enhanced viral replication and severe disease. One group of cross-reactive antibodies that contributes considerably to this serum profile target the premembrane (prM) protein. We report here the isolation of a large panel of naturally occurring human monoclonal antibodies (MAbs) obtained from subjects following primary DENV serotype 1, 2, or 3 or secondary natural DENV infections or following primary DENV serotype 1 live attenuated virus vaccination to determine the antigenic landscape on the prM protein that is recognized by human antibodies. We isolated 25 prM-reactive human MAbs, encoded by diverse antibody-variable genes. Competition-binding studies revealed that all of the antibodies bound to a single major antigenic site on prM. Alanine scanning-based shotgun mutagenesis epitope mapping studies revealed diverse patterns of fine specificity of various clones, suggesting that different antibodies use varied binding poses to recognize several overlapping epitopes within the immunodominant site. Several of the antibodies interacted with epitopes on both prM and E protein residues. Despite the diverse genetic origins of the antibodies and differences in the fine specificity of their epitopes, each of these prM-reactive antibodies was capable of enhancing the DENV infection of Fc receptor-bearing cells., Importance: Antibodies may play a critical role in the pathogenesis of enhanced DENV infection and disease during secondary infections. A substantial proportion of enhancing antibodies generated in response to natural dengue infection are directed toward the prM protein. The fine specificity of human prM antibodies is not understood. Here, we isolated a panel of dengue prM-specific human monoclonal antibodies from individuals after infection in order to define the mode of molecular recognition by enhancing antibodies. We found that only a single antibody molecule can be bound to each prM protein at any given time. Distinct overlapping epitopes were mapped, but all of the epitopes lie within a single major antigenic site, suggesting that this antigenic domain forms an immunodominant region of the protein. Neutralization and antibody-dependent enhanced replication experiments showed that recognition of any of the epitopes within the major antigenic site on prM was sufficient to cause enhanced infection of target cells., (Copyright © 2015, American Society for Microbiology. All Rights Reserved.)

Published
2015
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