Found 1 matching record:
Displaying record number 3656
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MAb ID |
DH511.2 (DH512, Ab510049) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Epitope |
|
Subtype |
C |
Ab Type |
gp41 MPER (membrane proximal external region) |
Neutralizing |
P (tier 2) View neutralization details |
Contacts and Features |
View contacts and features |
Species
(Isotype)
|
human(IgG) |
Patient |
CH0210 |
Immunogen |
HIV-1 infection |
Country |
South Africa |
Keywords |
acute/early infection, antibody binding site, antibody generation, antibody lineage, antibody polyreactivity, antibody sequence, broad neutralizer, computational prediction, contact residues, germline, mother-to-infant transmission, neutralization, structure, transmission pair, vaccine antigen design |
Notes
Showing 6 of
6 notes.
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DH512: HIV-1 env genes were sequenced from 16 mother/infant transmitting pairs. Infant transmitted-founder (T/F) and representative maternal non-transmitted Env variants were identified and used to generate pseudoviruses for paired maternal plasma neutralization analysis. Eighteen out of 21 (85%) infant T/F Env pseudoviruses were neutralization resistant to paired maternal plasma, while all infant T/F viruses were neutralization sensitive to a panel of HIV-1 broadly neutralizing antibodies (2G12, CH01, PG9, PG16, PGT121, PGT126, DH429, b12, VRC01, NIH45-46, CH31, 4E10, 2F5, 10E8, DH512) and variably sensitive to heterologous plasma neutralizing antibodies. Antibody mixture CH01/31 was used as a positive control for neutralization. The infant T/F pseudoviruses were overall more neutralization resistant to paired maternal plasma in comparison to pseudoviruses from maternal non-transmitted variants. These findings suggest that autologous neutralization of circulating viruses by maternal plasma antibodies select for neutralization-resistant viruses that initiate peripartum transmission, raising the speculation that enhancement of this response at the end of pregnancy could reduce infant HIV-1 infection risk.
Kumar2018
(neutralization, acute/early infection, mother-to-infant transmission, transmission pair)
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DH511.2: HIV-1 bnAbs require high levels of activation-induced cytidine deaminase (AID)-catalyzed somatic mutations. Probable mutations occur at sites of frequent AID activity, while improbable mutations occur where AID activity is infrequent. The paper introduced the ARMADiLLO program, which estimates how probable a particular mAb mutation is, and thus the key improbable mutations were defined for a panel of 26 bnAbs. The number of improbable mutations ranged from 7 (PGT128) to 23 (VRC01 and 35O22); DH511.2 had 19 improbable mutations out of 46 total AA mutations, and 0 indels. Single-amino acid reversion mutants were made for key improbable mutations of 3 bnAbs (CH235, VRC01, and BF520.1), and these mutant mAbs were tested for their neutralization ability. The study also noted that bnAbs that had relatively small numbers of improbable single somatic mutations had other unusual characteristics that were due to additional improbable events, such as indels (PGT128) or extraordinary CDR H3 lengths (VRC26.25).
Wiehe2018
(neutralization)
-
DH511.2: Plasma from donor PG13 was found to have MPER neutralization activity, and mAb PGZL1 was isolated. When compared to a 4E10, PGZL1 was found to share similar crystal structure, contacts, and some common germline genes, but its neutralization and polyreactivity were less strong. The germline gene usage of PGZL1 was compared with other MPER antibodies: 4E10, VRC42.01, 10E8, DH511.2, DH517, Z13, and 2F5.
Zhang2019a
(neutralization, structure, contact residues, germline)
-
DH511.2: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of nAb responses compared with Env 459C alone. DH511.2 was used for analyzing clade sensitivity.
Bricault2019
(antibody binding site, neutralization, vaccine antigen design, computational prediction, broad neutralizer)
-
DH511.2: Six clonally related mAbs, designated DH511.1 to DH511.6 were isolated by single memory B cell sorting from a clade-C-infected African donor, CH0210. Among them, DH511.2 had the most potent neutralization. Several additional antibodies were derived from the patient's plasma and designated DH511.7P - DH511.12P. In a panel of 208 HIV-1 isolates, DH511.11P and DH511.12P had slightly increased breadth and potency compared with DH511.2. Thirty-five chimeric mAbs were produced by swapping the heavy and light chains of DH511.2 with those of plasma DH511 lineage members; among these, DH511.2-K3 had the highest potency.
Williams2017
(antibody generation, neutralization, antibody sequence, structure, antibody lineage, antibody polyreactivity, broad neutralizer)
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DH511.2: This patent application describes MPER antibody lineages DH511, DH512, DH513, DH514, DH515, DH516, DH517, DH518, DH536, DH537, DH491, DH493 and derivative antibodies. Lineages DH511-517 were derived from donor CH0210. DH511.2 is a mAb in the DH511 lineage. This patent application lists some name aliases as follows: "Various antibodies names are used throughout the application. Antibodies names correlation is as follows: Memory B cell antibodies: DH511=DH511.1; DH512=DH511.2; DH513=DH511.3; DH514=DH511.4; DH515=DH511.5; DH516=DH511.6; Plasma antibodies: DH511 la=DH511.7P; DH511 2a=DH511.8P; DH511 3a=DH511.9P; DH511 4a=DH511.10P; DH511 5a=DH511.11P; DH511 5a=DH511.12P." On the basis of this information, appropriate alias names have been added in LANL antibody database.
Haynes2016a
(neutralization, antibody lineage)
References
Showing 6 of
6 references.
Isolation Paper
Williams2017
LaTonya D. Williams, Gilad Ofek, Sebastian Schätzle, Jonathan R. McDaniel, Xiaozhi Lu, Nathan I. Nicely, Liming Wu, Caleb S. Lougheed, Todd Bradley, Mark K. Louder, Krisha McKee, Robert T. Bailer, Sijy O'Dell, Ivelin S. Georgiev, Michael S. Seaman, Robert J. Parks, Dawn J. Marshall, Kara Anasti, Guang Yang, Xiaoyan Nie, Nancy L. Tumba, Kevin Wiehe, Kshitij Wagh, Bette Korber, Thomas B. Kepler, S. Munir Alam, Lynn Morris, Gift Kamanga, Myron S. Cohen, Mattia Bonsignori, Shi-Mao Xia, David C. Montefiori, Garnett Kelsoe, Feng Gao, John R. Mascola, M. Anthony Moody, Kevin O. Saunders, Hua-Xin Liao, Georgia D. Tomaras, George Georgiou, and Barton F. Haynes. Potent and Broad HIV-Neutralizing Antibodies in Memory B Cells and Plasma. Sci. Immunol., 2(7), 27 Jan 2017. PubMed ID: 28783671.
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Bricault2019
Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920.
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Haynes2016a
B. F. Haynes, H. X. Liao, M. A. Moody, L. Williams, K. J. Wiehe, and G. A. Ofek. HIV-1 Neutralizing Antibodies and Uses Thereof. WIPO patent application, Sep 2016. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2016149710. Application number PCT/US2016/023488.
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Kumar2018
Amit Kumar, Claire E. P. Smith, Elena E. Giorgi, Joshua Eudailey, David R. Martinez, Karina Yusim, Ayooluwa O. Douglas, Lisa Stamper, Erin McGuire, Celia C. LaBranche, David C. Montefiori, Genevieve G. Fouda, Feng Gao, and Sallie R. Permar. Infant Transmitted/Founder HIV-1 Viruses from Peripartum Transmission Are Neutralization Resistant to Paired Maternal Plasma. PLoS Pathog., 14(4):e1006944, Apr 2018. PubMed ID: 29672607.
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Wiehe2018
Kevin Wiehe, Todd Bradley, R. Ryan Meyerhoff, Connor Hart, Wilton B. Williams, David Easterhoff, William J. Faison, Thomas B. Kepler, Kevin O. Saunders, S. Munir Alam, Mattia Bonsignori, and Barton F. Haynes. Functional Relevance of Improbable Antibody Mutations for HIV Broadly Neutralizing Antibody Development. Cell Host Microbe, 23(6):759-765.e6, 13 Jun 2018. PubMed ID: 29861171.
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Zhang2019a
Lei Zhang, Adriana Irimia, Lingling He, Elise Landais, Kimmo Rantalainen, Daniel P. Leaman, Thomas Vollbrecht, Armando Stano, Daniel I. Sands, Arthur S. Kim, IAVI Protocol G Investigators, Pascal Poignard, Dennis R. Burton, Ben Murrell, Andrew B. Ward, Jiang Zhu, Ian A. Wilson, and Michael B. Zwick. An MPER Antibody Neutralizes HIV-1 Using Germline Features Shared Among Donors. Nat. Commun., 10(1):5389, 26 Nov 2019. PubMed ID: 31772165.
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