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Article ; Online: Exploiting

Wibmer, Constantinos Kurt / Mashilo, Poppy

2022 Volume 14, Issue 10

Abstract: Horses and humans share a close relationship that includes both species' viromes. Many emerging infectious diseases can be transmitted between horses and humans and can exhibit mortality rates as high as 90% in both populations. Antibody biologics ... ...

Abstract	Horses and humans share a close relationship that includes both species' viromes. Many emerging infectious diseases can be transmitted between horses and humans and can exhibit mortality rates as high as 90% in both populations. Antibody biologics represents an emerging field of rapidly discoverable and potent antiviral therapeutics. These biologics can be used to provide passive immunity, as well as blueprints for the rational design of novel active vaccine antigens. Here, we exploit the limited diversity of immunoglobulin variable genes used by horses to develop a rapid, high-throughput monoclonal antibody discovery pipeline. The antibodies isolated from two horses in this study were developed with near exclusivity from a few highly related germline genes within a single IgHV and IgλV gene family and could be recovered for cloning with just three primer pairs. This variable gene pairing was compatible with both horse and human immunoglobulin G isotypes, confirming the suitability of an equine antibody discovery pipeline for developing novel therapeutics to meet the One Health approach to infectious diseases.
MeSH term(s)	Horses ; Animals ; Humans ; Antibodies, Monoclonal ; Immunoglobulin G ; Biological Products ; Antiviral Agents ; Vaccines
Chemical Substances	Antibodies, Monoclonal ; Immunoglobulin G ; Biological Products ; Antiviral Agents ; Vaccines
Language	English
Publishing date	2022-09-30
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14102172
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Article ; Online: Neutralization Breadth and Potency of Single-Chain Variable Fragments Derived from Broadly Neutralizing Antibodies Targeting Multiple Epitopes on the HIV-1 Envelope.

van Dorsten, Rebecca T / Lambson, Bronwen E / Wibmer, Constantinos Kurt / Weinberg, Marc S / Moore, Penny L / Morris, Lynn

Journal of virology

2020 Volume 94, Issue 2

Abstract: Passive administration of HIV-directed broadly neutralizing antibodies (bNAbs) can prevent infection in animal models, and human efficacy trials are under way. Single-chain variable fragments (scFv), comprised of only the variable regions of antibody ... ...

Abstract	Passive administration of HIV-directed broadly neutralizing antibodies (bNAbs) can prevent infection in animal models, and human efficacy trials are under way. Single-chain variable fragments (scFv), comprised of only the variable regions of antibody heavy and light chains, are smaller molecules that may offer advantages over full-length IgG. We designed and expressed scFv of HIV bNAbs prioritized for clinical testing that target the V2-apex (CAP256-VRC26.25), V3-glycan supersite (PGT121), CD4 binding site (3BNC117), and MPER (10E8v4). The use of either a 15- or 18-amino-acid glycine-serine linker between the heavy- and light-chain fragments provided adequate levels of scFv expression. When tested against a 45-multisubtype virus panel, all four scFv retained good neutralizing activity, although there was variable loss of function compared to the parental IgG antibodies. For CAP256-VRC26.25, there was a significant 138-fold loss of potency that was in part related to differential interaction with charged amino acids at positions 169 and 170 in the V2 epitope. Potency was reduced for the 3BNC117 (13-fold) and PGT121 (4-fold) scFv among viruses lacking the N276 and N332 glycans, respectively, and in viruses with a longer V1 loop for PGT121. This suggested that scFv interacted with their epitopes in subtly different ways, with variation at key residues affecting scFv neutralization more than the matched IgGs. Remarkably, the scFv of 10E8v4 maintained breadth of 100% with only a minor reduction in potency. Overall, scFv of clinically relevant bNAbs had significant neutralizing activity, indicating that they are suitable for passive immunization to prevent HIV-1 infection.
MeSH term(s)	Antibodies, Neutralizing/immunology ; Antibody Specificity ; HIV Antibodies/immunology ; HIV Envelope Protein gp160/immunology ; HIV-1/immunology ; Humans ; Single-Chain Antibodies/immunology
Chemical Substances	Antibodies, Neutralizing ; HIV Antibodies ; HIV Envelope Protein gp160 ; Single-Chain Antibodies
Language	English
Publishing date	2020-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01533-19
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Article ; Online: HIV broadly neutralizing antibody targets.

Wibmer, Constantinos Kurt / Moore, Penny L / Morris, Lynn

Current opinion in HIV and AIDS

2015 Volume 10, Issue 3, Page(s) 135–143

Abstract: Purpose of review: To provide an update on neutralizing antibody targets in the context of the recent HIV-1 envelope trimer structure, describe new antibody isolation technologies, and discuss the implications of these data for HIV-1 prevention and ... ...

Abstract	Purpose of review: To provide an update on neutralizing antibody targets in the context of the recent HIV-1 envelope trimer structure, describe new antibody isolation technologies, and discuss the implications of these data for HIV-1 prevention and therapy. Recent findings: Recent advances in B-cell technologies have dramatically expanded the number of antibodies isolated from HIV-infected donors with broadly neutralizing plasma activity. These, together with the first high-resolution crystal and cryo-electron microscopy (cryo-EM) structures of a cleaved, prefusion HIV-1 trimer, have defined new regions susceptible to neutralization. This year, three epitopes in the gp120-gp41 interface were structurally characterized, highlighting the importance of prefusion gp41 as a target. Similar to many other broadly neutralizing antibody epitopes, these new antibodies define a target that is also highly glycan dependent. Collectively, the epitopes for broadly neutralizing antibodies now reveal a continuum of vulnerability spanning the length of the HIV-1 envelope trimer. Summary: Progress in the last year has provided support for the use of rationally stabilized whole HIV-1 trimers as immunogens for eliciting antibodies to multiple epitopes. Furthermore, the increasing number of broad and potent antibodies with the potential for synergistic/complementary combinations opens up new avenues for preventing and treating HIV-1 infection.
MeSH term(s)	Antibodies, Neutralizing/immunology ; HIV Antibodies/immunology ; HIV Infections/immunology ; HIV-1/immunology ; Humans
Chemical Substances	Antibodies, Neutralizing ; HIV Antibodies
Language	English
Publishing date	2015-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.0000000000000153
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Article ; Online: Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions

Constantinos Kurt Wibmer / Simone I. Richardson / Jason Yolitz / Claudia Cicala / James Arthos / Penny L. Moore / Lynn Morris

Nature Communications, Vol 9, Iss 1, Pp 1-

2018 Volume 14

Abstract: ... with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound ...

Abstract	Antibodies blocking the V1V2 domain of HIV Envelope from binding integrin are associated with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound to these antibodies, revealing an alternative fold of V1V2 with exposed integrin-binding sites that functions on non-native Envelope.
Keywords	Science ; Q
Language	English
Publishing date	2018-10-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions

Constantinos Kurt Wibmer / Simone I. Richardson / Jason Yolitz / Claudia Cicala / James Arthos / Penny L. Moore / Lynn Morris

Nature Communications, Vol 9, Iss 1, Pp 1-

2018 Volume 14

Abstract: ... with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound ...

Abstract	Antibodies blocking the V1V2 domain of HIV Envelope from binding integrin are associated with positive disease outcomes. Here, Wibmer et al. determine the structure of full length V1V2 bound to these antibodies, revealing an alternative fold of V1V2 with exposed integrin-binding sites that functions on non-native Envelope.
Keywords	Science ; Q
Language	English
Publishing date	2018-10-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Genome Sequencing of a Severe Acute Respiratory Syndrome Coronavirus 2 Isolate Obtained from a South African Patient with Coronavirus Disease 2019.

Allam, Mushal / Ismail, Arshad / Khumalo, Zamantungwa T H / Kwenda, Stanford / van Heusden, Peter / Cloete, Ruben / Wibmer, Constantinos Kurt / Mtshali, Phillip Senzo / Mnyameni, Florah / Mohale, Thabo / Subramoney, Kathleen / Walaza, Sibongile / Ngubane, Wendy / Govender, Nevashan / Motaze, Nkengafac V / Bhiman, Jinal N

Microbiology resource announcements

2020 Volume 9, Issue 27

Abstract: As a contribution to the global efforts to track and trace the ongoing coronavirus pandemic, here we present the sequence, phylogenetic analysis, and modeling of nonsynonymous mutations for a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) ... ...

Abstract	As a contribution to the global efforts to track and trace the ongoing coronavirus pandemic, here we present the sequence, phylogenetic analysis, and modeling of nonsynonymous mutations for a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome that was detected in a South African patient with coronavirus disease 2019 (COVID-19).
Keywords	covid19
Language	English
Publishing date	2020-07-02
Publishing country	United States
Document type	Journal Article
ISSN	2576-098X
ISSN (online)	2576-098X
DOI	10.1128/MRA.00572-20
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Article ; Online: Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions.

Wibmer, Constantinos Kurt / Richardson, Simone I / Yolitz, Jason / Cicala, Claudia / Arthos, James / Moore, Penny L / Morris, Lynn

Nature communications

2018 Volume 9, Issue 1, Page(s) 4489

Abstract: The α4β7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated lymphoid tissues. Antibodies blocking this interaction early in infection can improve disease outcome, ...

Abstract	The α4β7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated lymphoid tissues. Antibodies blocking this interaction early in infection can improve disease outcome, and V1V2-targeted antibodies were correlated with moderate efficacy reported from the RV144 HIV-1 vaccine trial. Monoclonal α4β7-blocking antibodies recognise two slightly different helical V2 conformations, and current structural data suggests their binding sites are occluded in prefusion envelope trimers. Here, we report cocrystal structures of two α4β7-blocking antibodies from an infected donor complexed with scaffolded V1V2 or V2 peptides. Both antibodies recognised the same helix-coil V2 conformation as RV144 antibody CH58, identifying a frequently sampled alternative conformation of full-length V1V2. In the context of Envelope, this α-helical form of V1V2 displays highly exposed α4β7-binding sites, potentially providing a functional role for non-native Envelope on virion or infected cell surfaces in HIV-1 dissemination, pathogenesis, and vaccine design.
MeSH term(s)	Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Binding Sites ; Epitopes/chemistry ; HIV Antibodies/immunology ; HIV Antibodies/metabolism ; HIV Envelope Protein gp120/chemistry ; HIV Envelope Protein gp120/immunology ; HIV Envelope Protein gp120/metabolism ; HIV Infections/immunology ; HIV-1/immunology ; HIV-1/metabolism ; Humans ; Integrins/antagonists & inhibitors ; Integrins/chemistry ; Integrins/metabolism ; Protein Binding/immunology ; Protein Conformation ; Receptors, HIV/antagonists & inhibitors ; Receptors, HIV/chemistry ; Receptors, HIV/metabolism ; Virion/metabolism
Chemical Substances	Antibodies, Monoclonal ; Epitopes ; HIV Antibodies ; HIV Envelope Protein gp120 ; Integrins ; Receptors, HIV ; integrin alpha4beta7
Language	English
Publishing date	2018-10-26
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-018-06794-x
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Article: SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma.

Wibmer, Constantinos Kurt / Ayres, Frances / Hermanus, Tandile / Madzivhandila, Mashudu / Kgagudi, Prudence / Oosthuysen, Brent / Lambson, Bronwen E / de Oliveira, Tulio / Vermeulen, Marion / van der Berg, Karin / Rossouw, Theresa / Boswell, Michael / Ueckermann, Veronica / Meiring, Susan / von Gottberg, Anne / Cohen, Cheryl / Morris, Lynn / Bhiman, Jinal N / Moore, Penny L

bioRxiv : the preprint server for biology

2021

Abstract: SARS-CoV-2 501Y.V2 (B.1.351), a novel lineage of coronavirus causing COVID-19, contains substitutions in two immunodominant domains of the spike protein. Here, we show that pseudovirus expressing 501Y.V2 spike protein completely escapes three classes of ... ...

Abstract	SARS-CoV-2 501Y.V2 (B.1.351), a novel lineage of coronavirus causing COVID-19, contains substitutions in two immunodominant domains of the spike protein. Here, we show that pseudovirus expressing 501Y.V2 spike protein completely escapes three classes of therapeutically relevant antibodies. This pseudovirus also exhibits substantial to complete escape from neutralization, but not binding, by convalescent plasma. These data highlight the prospect of reinfection with antigenically distinct variants and foreshadows reduced efficacy of spike-based vaccines.
Language	English
Publishing date	2021-03-01
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.01.18.427166
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Article ; Online: SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma.

Nature medicine

2021 Volume 27, Issue 4, Page(s) 622–625

Abstract	SARS-CoV-2 501Y.V2 (B.1.351), a novel lineage of coronavirus causing COVID-19, contains substitutions in two immunodominant domains of the spike protein. Here, we show that pseudovirus expressing 501Y.V2 spike protein completely escapes three classes of therapeutically relevant antibodies. This pseudovirus also exhibits substantial to complete escape from neutralization, but not binding, by convalescent plasma. These data highlight the prospect of reinfection with antigenically distinct variants and foreshadows reduced efficacy of spike-based vaccines.
MeSH term(s)	Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Blood Donors ; COVID-19/immunology ; COVID-19 Vaccines/immunology ; Humans ; Immune Evasion ; Neutralization Tests ; SARS-CoV-2/immunology ; Spike Glycoprotein, Coronavirus/immunology
Chemical Substances	Antibodies, Viral ; COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2021-03-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/s41591-021-01285-x
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Article ; Online: A combination of potently neutralizing monoclonal antibodies isolated from an Indian convalescent donor protects against the SARS-CoV-2 Delta variant.

Hingankar, Nitin / Deshpande, Suprit / Das, Payel / Rizvi, Zaigham Abbas / Wibmer, Constantinos Kurt / Mashilo, Poppy / Ansari, Mohammed Yousuf / Burns, Alison / Barman, Shawn / Zhao, Fangzhu / Mukherjee, Sohini / Torres, Jonathan L / Chattopadhyay, Souvick / Mehdi, Farha / Sutar, Jyoti / Rathore, Deepak Kumar / Pargai, Kamal / Singh, Janmejay / Sonar, Sudipta /

Jakhar, Kamini / Dandotiya, Jyotsna / Bhattacharyya, Sankar / Mani, Shailendra / Samal, Sweety / Singh, Savita / Kshetrapal, Pallavi / Thiruvengadam, Ramachandran / Batra, Gaurav / Medigeshi, Guruprasad / Ward, Andrew B / Bhatnagar, Shinjini / Awasthi, Amit / Sok, Devin / Bhattacharya, Jayanta

PLoS pathogens

2022 Volume 18, Issue 4, Page(s) e1010465

Abstract: Although efficacious vaccines have significantly reduced the morbidity and mortality of COVID-19, there remains an unmet medical need for treatment options, which monoclonal antibodies (mAbs) can potentially fill. This unmet need is exacerbated by the ... ...

Abstract	Although efficacious vaccines have significantly reduced the morbidity and mortality of COVID-19, there remains an unmet medical need for treatment options, which monoclonal antibodies (mAbs) can potentially fill. This unmet need is exacerbated by the emergence and spread of SARS-CoV-2 variants of concern (VOCs) that have shown some resistance to vaccine responses. Here we report the isolation of five neutralizing mAbs from an Indian convalescent donor, out of which two (THSC20.HVTR04 and THSC20.HVTR26) showed potent neutralization of SARS-CoV-2 VOCs at picomolar concentrations, including the Delta variant (B.1.617.2). One of these (THSC20.HVTR26) also retained activity against the Omicron variant. These two mAbs target non-overlapping epitopes on the receptor-binding domain (RBD) of the spike protein and prevent virus attachment to its host receptor, human angiotensin converting enzyme-2 (hACE2). Furthermore, the mAb cocktail demonstrated protection against the Delta variant at low antibody doses when passively administered in the K18 hACE2 transgenic mice model, highlighting their potential as a cocktail for prophylactic and therapeutic applications. Developing the capacity to rapidly discover and develop mAbs effective against highly transmissible pathogens like coronaviruses at a local level, especially in a low- and middle-income country (LMIC) such as India, will enable prompt responses to future pandemics as an important component of global pandemic preparedness.
MeSH term(s)	Animals ; Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19/prevention & control ; Mice ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-04-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010465
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