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Article ; Online: Protocol to identify and monitor key mutations of broadly neutralizing antibody lineages following sequential immunization of Ig-humanized mice.

Chen, Xuejun / Schmidt, Stephen D / Duan, Hongying / Doria-Rose, Nicole A / Mascola, John R

STAR protocols

2022 Volume 3, Issue 1, Page(s) 101180

Abstract: Using the VRC01-class of anti-HIV-1 broadly neutralizing antibodies (bnAbs) elicited in sequentially immunized Ig-humanized mice as an example, we describe a protocol to identify key mutations for bnAb function by point mutagenesis and antibody binding ... ...

Abstract	Using the VRC01-class of anti-HIV-1 broadly neutralizing antibodies (bnAbs) elicited in sequentially immunized Ig-humanized mice as an example, we describe a protocol to identify key mutations for bnAb function by point mutagenesis and antibody binding and neutralization assays. We also describe steps to monitor how the key mutations arise in response to specific immunogens, which is critical for vaccine evaluation and design, via longitudinal antibody mutation profiling. This protocol can be customized for other V-gene-specific bnAbs and animal models. For complete details on the use and execution of this profile, please refer to Chen et al. (2021).
MeSH term(s)	Animals ; Antibodies, Neutralizing ; Broadly Neutralizing Antibodies ; HIV Antibodies ; HIV Infections ; HIV-1/genetics ; Immunization ; Immunoglobulins/immunology ; Mice ; Mutation
Chemical Substances	Antibodies, Neutralizing ; Broadly Neutralizing Antibodies ; HIV Antibodies ; Immunoglobulins
Language	English
Publishing date	2022-02-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	2666-1667
ISSN (online)	2666-1667
DOI	10.1016/j.xpro.2022.101180
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Article ; Online: Coevolution of HIV-1 and broadly neutralizing antibodies.

Doria-Rose, Nicole A / Landais, Elise

Current opinion in HIV and AIDS

2019 Volume 14, Issue 4, Page(s) 286–293

Abstract: Purpose of review: Exploring the molecular details of the coevolution of HIV-1 Envelope with broadly neutralizing antibodies (bNAbs) in infected individuals over time provides insights for vaccine design. Since mid-2017, the number of individuals ... ...

Abstract	Purpose of review: Exploring the molecular details of the coevolution of HIV-1 Envelope with broadly neutralizing antibodies (bNAbs) in infected individuals over time provides insights for vaccine design. Since mid-2017, the number of individuals described in such publications has nearly tripled. New publications have extended such studies to new epitopes on Env and provided more detail on previously known sites. Recent findings: Studies of two donors - one of them an infant, the other with three lineages targeting the same site - has deepened our understanding of V3-glycan-directed lineages. A V2-apex-directed lineage showed remarkable similarity to a lineage from a previously described donor, revealing general principles for this class of bNAbs. Understanding development of CD4 binding site antibodies has been enriched by the study of a VRC01-class lineage. Finally, the membrane-proximal external region is a new addition to the set of epitopes studied in this manner, with early development events explored in a study of three lineages from a single donor. Summary: These studies provide templates for immunogen design to elicit bNAbs against a widened set of epitopes, generating new directions in the quest for an HIV vaccine.
MeSH term(s)	Animals ; Biological Coevolution ; Broadly Neutralizing Antibodies/immunology ; Epitopes/genetics ; Epitopes/immunology ; HIV Antibodies/immunology ; HIV Infections/immunology ; HIV Infections/virology ; HIV-1/genetics ; HIV-1/immunology ; Humans
Chemical Substances	Broadly Neutralizing Antibodies ; Epitopes ; HIV Antibodies
Language	English
Publishing date	2019-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2502511-9
ISSN	1746-6318 ; 1746-630X
ISSN (online)	1746-6318
ISSN	1746-630X
DOI	10.1097/COH.0000000000000550
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Article ; Online: Protocol to identify and monitor key mutations of broadly neutralizing antibody lineages following sequential immunization of Ig-humanized mice

Xuejun Chen / Stephen D. Schmidt / Hongying Duan / Nicole A. Doria-Rose / John R. Mascola

STAR Protocols, Vol 3, Iss 1, Pp 101180- (2022)

2022

Abstract: Summary: Using the VRC01-class of anti-HIV-1 broadly neutralizing antibodies (bnAbs) elicited in sequentially immunized Ig-humanized mice as an example, we describe a protocol to identify key mutations for bnAb function by point mutagenesis and antibody ... ...

Abstract	Summary: Using the VRC01-class of anti-HIV-1 broadly neutralizing antibodies (bnAbs) elicited in sequentially immunized Ig-humanized mice as an example, we describe a protocol to identify key mutations for bnAb function by point mutagenesis and antibody binding and neutralization assays. We also describe steps to monitor how the key mutations arise in response to specific immunogens, which is critical for vaccine evaluation and design, via longitudinal antibody mutation profiling. This protocol can be customized for other V-gene-specific bnAbs and animal models.For complete details on the use and execution of this profile, please refer to Chen et al. (2021).
Keywords	Bioinformatics ; Sequence analysis ; Flow Cytometry/Mass Cytometry ; Immunology ; Model Organisms ; Molecular Biology ; Science (General) ; Q1-390
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: HIV neutralizing antibodies: clinical correlates and implications for vaccines.

Doria-Rose, Nicole A

The Journal of infectious diseases

2010 Volume 201, Issue 7, Page(s) 981–983

MeSH term(s)	AIDS Vaccines/immunology ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; HIV Infections/immunology ; HIV Infections/prevention & control ; HIV Infections/virology ; HIV-1/immunology ; Humans
Chemical Substances	AIDS Vaccines ; Antibodies, Neutralizing ; Antibodies, Viral
Language	English
Publishing date	2010-02-19
Publishing country	United States
Document type	Comment ; Editorial
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1086/651143
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Zs.MO 445: Show issues

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Article ; Online: Frequency-potency analysis of IgG+ memory B cells delineates neutralizing antibody responses at single-cell resolution.

Cell reports

2024 Volume 43, Issue 3, Page(s) 113948

Abstract: Identifying individual functional B cell receptors (BCRs) is common, but two-dimensional analysis of B cell frequency versus BCR potency would delineate both quantity and quality of antigen-specific memory B cells. We efficiently determine quantitative ... ...

Abstract	Identifying individual functional B cell receptors (BCRs) is common, but two-dimensional analysis of B cell frequency versus BCR potency would delineate both quantity and quality of antigen-specific memory B cells. We efficiently determine quantitative BCR neutralizing activities using a single-cell-derived antibody supernatant analysis (SCAN) workflow and develop a frequency-potency algorithm to estimate B cell frequencies at various neutralizing activity or binding affinity cutoffs. In an HIV-1 fusion peptide (FP) immunization study, frequency-potency curves elucidate the quantity and quality of FP-specific immunoglobulin G (IgG)+ memory B cells for different animals, time points, and antibody lineages at single-cell resolution. The BCR neutralizing activities are mainly determined by their affinities to soluble envelope trimer. Frequency analysis definitively demonstrates dominant neutralizing antibody lineages. These findings establish SCAN and frequency-potency analyses as promising approaches for general B cell analysis and monoclonal antibody (mAb) discovery. They also provide specific rationales for HIV-1 FP-directed vaccine optimization.
MeSH term(s)	Animals ; Antibodies, Neutralizing ; HIV Antibodies ; Immunoglobulin G ; Memory B Cells ; HIV Seropositivity ; HIV-1 ; HIV Infections
Chemical Substances	Antibodies, Neutralizing ; HIV Antibodies ; Immunoglobulin G
Language	English
Publishing date	2024-03-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.113948
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Article ; Online: HIV Immunology Goes Out On a Limb.

Doria-Rose, Nicole A / Mascola, John R

Immunity

2016 Volume 44, Issue 5, Page(s) 1088–1090

Abstract: Vaccines against HIV most likely need to elicit broadly neutralizing antibodies. In this issue of Immunity, Poignard and colleagues describe the co-evolution of a broadly neutralizing antibody and the virus that triggered it, providing a template for HIV ...

Abstract	Vaccines against HIV most likely need to elicit broadly neutralizing antibodies. In this issue of Immunity, Poignard and colleagues describe the co-evolution of a broadly neutralizing antibody and the virus that triggered it, providing a template for HIV vaccine design.
MeSH term(s)	AIDS Vaccines/immunology ; Antibodies, Neutralizing/immunology ; HIV Antibodies/immunology ; HIV Infections/immunology ; HIV-1/immunology ; Humans
Chemical Substances	AIDS Vaccines ; Antibodies, Neutralizing ; HIV Antibodies
Language	English
Publishing date	2016--17
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2016.05.004
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Zs.A 4227: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 69: Show issues

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Article ; Online: Improved HIV-1 neutralization breadth and potency of V2-apex antibodies by in silico design.

Holt, Graham T / Gorman, Jason / Wang, Siyu / Lowegard, Anna U / Zhang, Baoshan / Liu, Tracy / Lin, Bob C / Louder, Mark K / Frenkel, Marcel S / McKee, Krisha / O'Dell, Sijy / Rawi, Reda / Shen, Chen-Hsiang / Doria-Rose, Nicole A / Kwong, Peter D / Donald, Bruce R

Cell reports

2023 Volume 42, Issue 7, Page(s) 112711

Abstract: Broadly neutralizing antibodies (bNAbs) against HIV can reduce viral transmission in humans, but an effective therapeutic will require unusually high breadth and potency of neutralization. We employ the OSPREY computational protein design software to ... ...

Abstract	Broadly neutralizing antibodies (bNAbs) against HIV can reduce viral transmission in humans, but an effective therapeutic will require unusually high breadth and potency of neutralization. We employ the OSPREY computational protein design software to engineer variants of two apex-directed bNAbs, PGT145 and PG9RSH, resulting in increases in potency of over 100-fold against some viruses. The top designed variants improve neutralization breadth from 39% to 54% at clinically relevant concentrations (IC
MeSH term(s)	Humans ; HIV Infections ; HIV Antibodies ; Antibodies, Neutralizing ; HIV-1 ; Broadly Neutralizing Antibodies ; Cryoelectron Microscopy ; HIV Seropositivity ; Neutralization Tests
Chemical Substances	HIV Antibodies ; Antibodies, Neutralizing ; Broadly Neutralizing Antibodies
Language	English
Publishing date	2023-07-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112711
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Article ; Online: Rhesus macaque Bcl-6/Bcl-xL B cell immortalization: Discovery of HIV-1 neutralizing antibodies from lymph node.

Samsel, Jakob / Boswell, Kristin L / Watkins, Timothy / Ambrozak, David R / Mason, Rosemarie / Yamamoto, Takuya / Ko, Sungyoul / Yang, Yongping / Zhou, Tongqing / Doria-Rose, Nicole A / Foulds, Kathryn E / Roederer, Mario / Mascola, John R / Kwong, Peter D / Gama, Lucio / Koup, Richard A

Journal of immunological methods

2023 Volume 516, Page(s) 113445

Abstract: Many HIV-1 vaccines are designed to elicit neutralizing antibodies, and pre-clinical testing is often carried out in rhesus macaques (RMs). We have therefore adapted a method of B cell immortalization for use with RM B cells. In this system, RM B cells ... ...

Abstract	Many HIV-1 vaccines are designed to elicit neutralizing antibodies, and pre-clinical testing is often carried out in rhesus macaques (RMs). We have therefore adapted a method of B cell immortalization for use with RM B cells. In this system, RM B cells are activated with CD40 ligand and RM IL-21 before transduction with a retroviral vector encoding Bcl-6, Bcl-xL, and green fluorescent protein. Importantly, RM B cells from lymph nodes are more effectively immortalized by this method than B cells from PBMC, a difference not seen in humans. We suggest the discrepancy between these two tissues is due to increased expression of CD40 on RM lymph node B cells. Immortalized RM B cells expand long-term, undergo minimal somatic hypermutation, express surface B cell receptor, and secrete antibodies into culture. This allows for the identification of cells based on antigen specificity and/or functional assays. Here, we show the characterization of this system and its application for the isolation of HIV-1 neutralizing antibodies from a SHIV.CH505-infected animal, both with and without antigen probe. Taken together, we show that Bcl-6/xL immortalization is a valuable and flexible tool for antibody discovery in RMs, but with important distinctions from application of the system in human cells.
MeSH term(s)	Animals ; Humans ; Macaca mulatta ; HIV-1 ; Leukocytes, Mononuclear ; HIV Antibodies ; Antibodies, Neutralizing ; AIDS Vaccines ; Lymph Nodes ; Simian Immunodeficiency Virus ; Simian Acquired Immunodeficiency Syndrome
Chemical Substances	HIV Antibodies ; Antibodies, Neutralizing ; AIDS Vaccines
Language	English
Publishing date	2023-02-25
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2023.113445
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Article ; Online: Analytical characterization of broadly neutralizing antibody CAP256LS heavy chain clipping during manufacturing development.

Gollapudi, Deepika / Rosales-Zavala, Erwin / Ivleva, Vera B / Yang, Yanhong / Li, Yile / O'Connell, Sarah / Doria-Rose, Nicole A / Patel, Aakash / Blackstock, Daniel / Gowetski, Daniel B / Carlton, Kevin / Gall, Jason G D / Lei, Q Paula

Biotechnology progress

2022 , Page(s) e3296

Abstract: Broadly neutralizing antibody (bNAb) CAP256-VRC26.25 (abbreviated CAP256LS), a human IgGI monoclonal antibody targeting the V1V2 site of the HIV-1 envelope, has demonstrated high therapeutic potential as a broadly neutralizing monoclonal antibody against ...

Abstract	Broadly neutralizing antibody (bNAb) CAP256-VRC26.25 (abbreviated CAP256LS), a human IgGI monoclonal antibody targeting the V1V2 site of the HIV-1 envelope, has demonstrated high therapeutic potential as a broadly neutralizing monoclonal antibody against HIV-1. During the process development, a heavy chain fragmentation (clipping) was observed, that led to a relative potency reduction. In this report, we highlighted a series of process and product mitigation strategies deployed to advance this product. We have detailed how analytical characterization tools, especially the microchip reduced capillary gel electrophoresis (CGE-SDS), played a pivotal role in identifying the development issues and in providing measurements to guide implementation of mitigation strategies.
Language	English
Publishing date	2022-08-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	165657-0
ISSN	1520-6033 ; 8756-7938
ISSN (online)	1520-6033
ISSN	8756-7938
DOI	10.1002/btpr.3296
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Article ; Online: Binding and neutralizing antibody responses to SARS-CoV-2 in very young children exceed those in adults.

Karron, Ruth A / Garcia Quesada, Maria / Schappell, Elizabeth A / Schmidt, Stephen D / Deloria Knoll, Maria / Hetrich, Marissa K / Veguilla, Vic / Doria-Rose, Nicole / Dawood, Fatimah S

JCI insight

2022 Volume 7, Issue 8

Abstract: BackgroundSARS-CoV-2 infections are frequently milder in children than adults, suggesting that immune responses may vary with age. However, information is limited regarding SARS-CoV-2 immune responses in young children.MethodsWe compared receptor binding ...

Abstract	BackgroundSARS-CoV-2 infections are frequently milder in children than adults, suggesting that immune responses may vary with age. However, information is limited regarding SARS-CoV-2 immune responses in young children.MethodsWe compared receptor binding domain-binding antibody (RBDAb) titers and SARS-CoV-2-neutralizing antibody titers, measured by pseudovirus-neutralizing antibody assay in serum specimens obtained from children aged 0-4 years and 5-17 years and in adults aged 18-62 years at the time of enrollment in a prospective longitudinal household study of SARS-CoV-2 infection.ResultsAmong 56 seropositive participants at enrollment, children aged 0-4 years had more than 10-fold higher RBDAb titers than adults (416 vs. 31, P < 0.0001) and the highest RBDAb titers in 11 of 12 households with seropositive children and adults. Children aged 0-4 years had only 2-fold higher neutralizing antibody than adults, resulting in higher binding-to-neutralizing antibody ratios compared with adults (2.36 vs. 0.35 for ID50, P = 0.0004).ConclusionThese findings suggest that young children mount robust antibody responses to SARS-CoV-2 following community infections. Additionally, these results support using neutralizing antibody to measure the immunogenicity of COVID-19 vaccines in children aged 0-4 years.FundingCDC (award 75D30120C08737).
MeSH term(s)	Adult ; Antibodies, Neutralizing ; Antibodies, Viral ; Antibody Formation ; COVID-19 ; COVID-19 Vaccines ; Child ; Child, Preschool ; Humans ; Prospective Studies ; SARS-CoV-2
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines
Language	English
Publishing date	2022-04-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.157963
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