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Article ; Online: Characterisation of Elevenin-Vc1 from the Venom of

Krishnarjuna, Bankala / Sunanda, Punnepalli / Seow, Jeffrey / Tae, Han-Shen / Robinson, Samuel D / Belgi, Alessia / Robinson, Andrea J / Safavi-Hemami, Helena / Adams, David J / Norton, Raymond S

Marine drugs

2023 Volume 21, Issue 2

Abstract: Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first ... ...

Abstract	Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail
MeSH term(s)	Mice ; Humans ; Animals ; Conotoxins/pharmacology ; Conus Snail/metabolism ; Venoms ; Receptors, Nicotinic/metabolism ; Peptides/metabolism ; Nicotinic Antagonists/pharmacology
Chemical Substances	Conotoxins ; Venoms ; Receptors, Nicotinic ; Peptides ; Nicotinic Antagonists
Language	English
Publishing date	2023-01-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2175190-0
ISSN	1660-3397 ; 1660-3397
ISSN (online)	1660-3397
ISSN	1660-3397
DOI	10.3390/md21020081
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Article ; Online: Broad and potent neutralizing antibodies are elicited in vaccinated individuals following Delta/BA.1 breakthrough infection.

Seow, Jeffrey / Shalim, Zayed A / Graham, Carl / Kimuda, Simon / Pillai, Aswin / Lechmere, Thomas / Kurshan, Ashwini / Khimji, Atika M / Snell, Luke B / Nebbia, Gaia / Mant, Christine / Waters, Anele / Fox, Julie / Malim, Michael H / Doores, Katie J

mBio

2023 Volume 14, Issue 5, Page(s) e0120623

Abstract: Importance: With the emergence of SARS-CoV-2 viral variants, there has been an increase in infections in vaccinated individuals. Here, we isolated monoclonal antibodies (mAbs) from individuals experiencing a breakthrough infection (Delta or BA.1) to ... ...

Abstract	Importance: With the emergence of SARS-CoV-2 viral variants, there has been an increase in infections in vaccinated individuals. Here, we isolated monoclonal antibodies (mAbs) from individuals experiencing a breakthrough infection (Delta or BA.1) to determine how exposure to a heterologous Spike broadens the neutralizing antibody response at the monoclonal level. All mAbs isolated had reactivity to the Spike of the vaccine and infection variant. While many mAbs showed reduced neutralization of current circulating variants, we identified mAbs with broad and potent neutralization of BA.2.75.2, XBB, XBB.1.5, and BQ.1.1 indicating the presence of conserved epitopes on Spike. These results indicate that variant-based vaccine boosters have the potential to broaden the vaccine response.
MeSH term(s)	Humans ; Breakthrough Infections ; Antibodies, Monoclonal ; Antibodies, Neutralizing ; Vaccines ; Antibodies, Viral
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Vaccines ; Antibodies, Viral
Language	English
Publishing date	2023-09-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.01206-23
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Article ; Online: Characterisation of Elevenin-Vc1 from the Venom of Conus victoriae: A Structural Analogue of α-Conotoxins

Krishnarjuna, Bankala / Sunanda, Punnepalli / Seow, Jeffrey / Tae, Han-Shen / Robinson, Samuel D. / Belgi, Alessia / Robinson, Andrea J. / Safavi-Hemami, Helena / Adams, David J. / Norton, Raymond S.

Mar Drugs. 2023 Jan. 25, v. 21, no. 2

2023

Abstract	Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail Conus victoriae (Gen. Comp. Endocrinol. 2017, 244, 11–18). Although numerous elevenin sequences have been reported, their physiological function is unclear, and no structural information is available. Upon intracranial injection in mice, elevenin-Vc1 induced hyperactivity at doses of 5 or 10 nmol. The structure of elevenin-Vc1, determined using nuclear magnetic resonance spectroscopy, consists of a short helix and a bend region stabilised by the single disulfide bond. The elevenin-Vc1 structural fold is similar to that of α-conotoxins such as α-RgIA and α-ImI, which are also found in the venoms of cone snails and are antagonists at specific subtypes of nicotinic acetylcholine receptors (nAChRs). In an attempt to mimic the functional motif, Asp-Pro-Arg, of α-RgIA and α-ImI, we synthesised an analogue, designated elevenin-Vc1-DPR. However, neither elevenin-Vc1 nor the analogue was active at six different human nAChR subtypes (α1β1δ, α3β2, α3β4, α4β2, α7, and α9α10) at 1 µM concentrations.
Keywords	Annelida ; Conus victoriae ; Nematoda ; acetylcholine ; amino acids ; disulfide bonds ; humans ; nuclear magnetic resonance spectroscopy ; peptides ; snails ; venoms
Language	English
Dates of publication	2023-0125
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article ; Online
ZDB-ID	2175190-0
ISSN	1660-3397
ISSN	1660-3397
DOI	10.3390/md21020081
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Broad Neutralization of SARS-CoV-2 Variants, Including Omicron, following Breakthrough Infection with Delta in COVID-19-Vaccinated Individuals.

Lechmere, Thomas / Snell, Luke B / Graham, Carl / Seow, Jeffrey / Shalim, Zayed A / Charalampous, Themoula / Alcolea-Medina, Adela / Batra, Rahul / Nebbia, Gaia / Edgeworth, Jonathan D / Malim, Michael H / Doores, Katie J

mBio

2022 Volume 13, Issue 2, Page(s) e0379821

Abstract: Numerous studies have shown that a prior SARS-CoV-2 infection can greatly enhance the antibody response to COVID-19 vaccination, with this so called "hybrid immunity" leading to greater neutralization breadth against SARS-CoV-2 variants of concern. ... ...

Abstract	Numerous studies have shown that a prior SARS-CoV-2 infection can greatly enhance the antibody response to COVID-19 vaccination, with this so called "hybrid immunity" leading to greater neutralization breadth against SARS-CoV-2 variants of concern. However, little is known about how breakthrough infection (BTI) in COVID-19-vaccinated individuals will impact the magnitude and breadth of the neutralizing antibody response. Here, we compared neutralizing antibody responses between unvaccinated and COVID-19-double-vaccinated individuals (including both AZD1222 and BNT162b2 vaccinees) who have been infected with the Delta (B.1.617.2) variant. Rapid production of spike-reactive IgG was observed in the vaccinated group, providing evidence of effective vaccine priming. Overall, potent cross-neutralizing activity against current SARS-CoV-2 variants of concern was observed in the BTI group compared to the infection group, including neutralization of the Omicron (B.1.1.529) variant. This study provides important insights into population immunity where transmission levels remain high and in the context of new or emerging variants of concern.
MeSH term(s)	Antibodies, Neutralizing ; Antibodies, Viral ; BNT162 Vaccine ; COVID-19/prevention & control ; COVID-19 Vaccines ; ChAdOx1 nCoV-19 ; Humans ; SARS-CoV-2/genetics
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; ChAdOx1 nCoV-19 (B5S3K2V0G8) ; BNT162 Vaccine (N38TVC63NU)
Language	English
Publishing date	2022-03-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.03798-21
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Article ; Online: A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination.

Seow, Jeffrey / Khan, Hataf / Rosa, Annachiara / Calvaresi, Valeria / Graham, Carl / Pickering, Suzanne / Pye, Valerie E / Cronin, Nora B / Huettner, Isabella / Malim, Michael H / Politis, Argyris / Cherepanov, Peter / Doores, Katie J

Cell reports

2022 Volume 40, Issue 8, Page(s) 111276

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is the target for neutralizing antibodies elicited following both infection and vaccination. While extensive research has shown that the receptor binding domain (RBD) and, to a lesser ... ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is the target for neutralizing antibodies elicited following both infection and vaccination. While extensive research has shown that the receptor binding domain (RBD) and, to a lesser extent, the N-terminal domain (NTD) are the predominant targets for neutralizing antibodies, identification of neutralizing epitopes beyond these regions is important for informing vaccine development and understanding antibody-mediated immune escape. Here, we identify a class of broadly neutralizing antibodies that bind an epitope on the spike subdomain 1 (SD1) and that have arisen from infection or vaccination. Using cryo-electron microscopy (cryo-EM) and hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS), we show that SD1-specific antibody P008_60 binds an epitope that is not accessible within the canonical prefusion states of the SARS-CoV-2 spike, suggesting a transient conformation of the viral glycoprotein that is vulnerable to neutralization.
MeSH term(s)	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 ; Cryoelectron Microscopy ; Epitopes ; Humans ; Neutralization Tests ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Syndactyly ; Vaccination
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-08-11
Publishing country	United States
Document type	Journal Article ; 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.2022.111276
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Article ; Online: Contrasting Modes of New World Arenavirus Neutralization by Immunization-Elicited Monoclonal Antibodies.

Ng, Weng M / Sahin, Mehmet / Krumm, Stefanie A / Seow, Jeffrey / Zeltina, Antra / Harlos, Karl / Paesen, Guido C / Pinschewer, Daniel D / Doores, Katie J / Bowden, Thomas A

mBio

2022 Volume 13, Issue 2, Page(s) e0265021

Abstract: Transmission of the New World hemorrhagic fever arenaviruses Junín virus (JUNV) and Machupo virus (MACV) to humans is facilitated, in part, by the interaction between the arenavirus GP1 glycoprotein and the human transferrin receptor 1 (hTfR1). We ... ...

Abstract	Transmission of the New World hemorrhagic fever arenaviruses Junín virus (JUNV) and Machupo virus (MACV) to humans is facilitated, in part, by the interaction between the arenavirus GP1 glycoprotein and the human transferrin receptor 1 (hTfR1). We utilize a mouse model of live-attenuated immunization with envelope exchange viruses to isolate neutralizing monoclonal antibodies (NAbs) specific to JUNV GP1 and MACV GP1. Structures of two NAbs, termed JUN1 and MAC1, demonstrate that they neutralize through disruption of hTfR1 recognition. JUN1 utilizes a binding mode common to all characterized infection- and vaccine-elicited JUNV-specific NAbs, which involves mimicking hTfR1 binding through the insertion of a tyrosine into the receptor-binding site. In contrast, MAC1 undergoes a tyrosine-mediated mode of antigen recognition distinct from that used by the reported anti-JUNV NAbs and the only other characterized anti-MACV NAb. These data reveal the varied modes of GP1-specific recognition among New World arenaviruses by the antibody-mediated immune response.
MeSH term(s)	Animals ; Antibodies, Monoclonal ; Antibodies, Neutralizing ; Arenaviruses, New World/metabolism ; Immunization ; Junin virus/metabolism ; Mice ; Receptors, Transferrin ; Tyrosine
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Receptors, Transferrin ; Tyrosine (42HK56048U)
Language	English
Publishing date	2022-03-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.02650-21
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Article ; Online: Disordered epitopes as peptide vaccines.

MacRaild, Christopher A / Seow, Jeffrey / Das, Sreedam C / Norton, Raymond S

Peptide science (Hoboken, N.J.)

2018 Volume 110, Issue 3, Page(s) e24067

Abstract: The development of clinically useful peptide-based vaccines remains a long-standing goal. This review highlights that intrinsically disordered protein antigens, which lack an ordered three-dimensional structure, represent excellent starting points for ... ...

Abstract	The development of clinically useful peptide-based vaccines remains a long-standing goal. This review highlights that intrinsically disordered protein antigens, which lack an ordered three-dimensional structure, represent excellent starting points for the development of such vaccines. Disordered proteins represent an important class of antigen in a wide range of human pathogens, and, contrary to widespread belief, they are frequently targets of protective antibody responses. Importantly, disordered epitopes appear invariably to be linear epitopes, rendering them ideally suited to incorporation into a peptide vaccine. Nonetheless, the conformational properties of disordered antigens, and hence their recognition by antibodies, frequently depend on the interactions they make and the context in which they are presented to the immune system. These effects must be considered in the design of an effective vaccine. Here we discuss these issues and propose design principles that may facilitate the development of peptide vaccines targeting disordered antigens.
Keywords	covid19
Language	English
Publishing date	2018-04-14
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2475-8817
ISSN (online)	2475-8817
DOI	10.1002/pep2.24067
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Article ; Online: Concordance of B- and T-cell responses to SARS-CoV-2 infection, irrespective of symptoms suggestive of COVID-19.

Österdahl, Marc F / Christakou, Eleni / Hart, Deborah / Harris, Ffion / Shahrabi, Yasaman / Pollock, Emily / Wadud, Muntaha / Spector, Tim D / Brown, Matthew A / Seow, Jeffrey / Malim, Michael H / Steves, Claire J / Doores, Katie J / Duncan, Emma L / Tree, Timothy

Journal of medical virology

2022 Volume 94, Issue 11, Page(s) 5217–5224

Abstract: This study assessed T-cell responses in individuals with and without a positive antibody response to SARS-CoV-2, in symptomatic and asymptomatic individuals during the COVID-19 pandemic. Participants were drawn from the TwinsUK cohort, grouped by (a) ... ...

Abstract	This study assessed T-cell responses in individuals with and without a positive antibody response to SARS-CoV-2, in symptomatic and asymptomatic individuals during the COVID-19 pandemic. Participants were drawn from the TwinsUK cohort, grouped by (a) presence or absence of COVID-associated symptoms (S+, S-), logged prospectively through the COVID Symptom Study app, and (b) anti-IgG Spike and anti-IgG Nucleocapsid antibodies measured by ELISA (Ab+, Ab-), during the first wave of the UK pandemic. T-cell helper and regulatory responses after stimulation with SARS-CoV-2 peptides were assessed. Thirty-two participants were included in the final analysis. Fourteen of 15 with IgG Spike antibodies had a T-cell response to SARS-CoV-2-specific peptides; none of 17 participants without IgG Spike antibodies had a T-cell response (χ
MeSH term(s)	Antibodies, Viral ; B-Lymphocytes ; COVID-19/diagnosis ; Humans ; Immunoglobulin G ; Pandemics ; RNA, Viral ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; T-Lymphocytes
Chemical Substances	Antibodies, Viral ; Immunoglobulin G ; RNA, Viral ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-07-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	752392-0
ISSN	1096-9071 ; 0146-6615
ISSN (online)	1096-9071
ISSN	0146-6615
DOI	10.1002/jmv.28016
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Article ; Online: The effect of Omicron breakthrough infection and extended BNT162b2 booster dosing on neutralization breadth against SARS-CoV-2 variants of concern.

Graham, Carl / Lechmere, Thomas / Rehman, Aisha / Seow, Jeffrey / Kurshan, Ashwini / Huettner, Isabella / Maguire, Thomas J A / Tam, Jerry C H / Cox, Daniel / Ward, Christopher / Racz, Mariusz / Waters, Anele / Mant, Christine / Malim, Michael H / Fox, Julie / Doores, Katie J

PLoS pathogens

2022 Volume 18, Issue 10, Page(s) e1010882

Abstract: COVID-19 vaccines are playing a vital role in controlling the COVID-19 pandemic. As SARS-CoV-2 variants encoding mutations in the surface glycoprotein, Spike, continue to emerge, there is increased need to identify immunogens and vaccination regimens ... ...

Abstract	COVID-19 vaccines are playing a vital role in controlling the COVID-19 pandemic. As SARS-CoV-2 variants encoding mutations in the surface glycoprotein, Spike, continue to emerge, there is increased need to identify immunogens and vaccination regimens that provide the broadest and most durable immune responses. We compared the magnitude and breadth of the neutralizing antibody response, as well as levels of Spike-reactive memory B cells, in individuals receiving a second dose of BNT162b2 at a short (3-4 week) or extended interval (8-12 weeks) and following a third vaccination approximately 6-8 months later. We show that whilst an extended interval between the first two vaccinations can greatly increase the breadth of the immune response and generate a higher proportion of Spike reactive memory B cells, a third vaccination leads to similar levels between the two groups. Furthermore, we show that the third vaccine dose enhances neutralization activity against omicron lineage members BA.1, BA.2 and BA.4/BA.5 and this is further increased following breakthrough infection during the UK omicron wave. These findings are relevant for vaccination strategies in populations where COVID-19 vaccine coverage remains low.
MeSH term(s)	Antibodies, Neutralizing ; Antibodies, Viral ; BNT162 Vaccine ; COVID-19/prevention & control ; COVID-19 Vaccines ; Humans ; Membrane Glycoproteins/genetics ; Pandemics ; SARS-CoV-2/genetics ; Vaccination ; Viral Vaccines
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Membrane Glycoproteins ; Viral Vaccines ; BNT162 Vaccine (N38TVC63NU)
Language	English
Publishing date	2022-10-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010882
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Article ; Online: ChAdOx1 nCoV-19 vaccine elicits monoclonal antibodies with cross-neutralizing activity against SARS-CoV-2 viral variants.

Seow, Jeffrey / Graham, Carl / Hallett, Sadie R / Lechmere, Thomas / Maguire, Thomas J A / Huettner, Isabella / Cox, Daniel / Khan, Hataf / Pickering, Suzanne / Roberts, Rebekah / Waters, Anele / Ward, Christopher C / Mant, Christine / Pitcher, Michael J / Spencer, Jo / Fox, Julie / Malim, Michael H / Doores, Katie J

Cell reports

2022 Volume 39, Issue 5, Page(s) 110757

Abstract: Although the antibody response to COVID-19 vaccination has been studied extensively at the polyclonal level using immune sera, little has been reported on the antibody response at the monoclonal level. Here, we isolate a panel of 44 anti-SARS-CoV-2 ... ...

Abstract	Although the antibody response to COVID-19 vaccination has been studied extensively at the polyclonal level using immune sera, little has been reported on the antibody response at the monoclonal level. Here, we isolate a panel of 44 anti-SARS-CoV-2 monoclonal antibodies (mAbs) from an individual who received two doses of the ChAdOx1 nCoV-19 (AZD1222) vaccine at a 12-week interval. We show that, despite a relatively low serum neutralization titer, Spike-reactive IgG+ B cells are still detectable 9 months post-boost. Furthermore, mAbs with potent neutralizing activity against the current SARS-CoV-2 variants of concern (Alpha, Gamma, Beta, Delta, and Omicron) are present. The vaccine-elicited neutralizing mAbs form eight distinct competition groups and bind epitopes overlapping with neutralizing mAbs elicited following SARS-CoV-2 infection. AZD1222-elicited mAbs are more mutated than mAbs isolated from convalescent donors 1-2 months post-infection. These findings provide molecular insights into the AZD1222 vaccine-elicited antibody response.
MeSH term(s)	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19/prevention & control ; COVID-19 Vaccines ; ChAdOx1 nCoV-19 ; Humans ; SARS-CoV-2 ; Vaccination
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; ChAdOx1 nCoV-19 (B5S3K2V0G8)
Language	English
Publishing date	2022-04-15
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.2022.110757
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