Handheld NIR-to-NIR Platform for on-site evaluating protective neutralizing antibody against SARS-CoV-2 ancestral strain and Omicron variant after vaccination or infection

Song, Qingwei; Zhao, Lei; Mai, Weikang; Xia, Daoyu; Ding, Weidong; Zhou, Xiaomian; Deng, Min; Lei, Yu; Chen, Lu; Li, Yantao; Mai, Xiaorui; Zhang, Lei; Chen, Zheng; Qin, Yiru; Ren, Ruiwen; Wei, Wei; Ji, Tianxing

doi:10.1016/j.bios.2023.115353

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Handheld NIR-to-NIR Platform for on-site evaluating protective neutralizing antibody against SARS-CoV-2 ancestral strain and Omicron variant after vaccination or infection

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Author(s): Qingwei Song ^a ^, ^b ^, ¹ , Lei Zhao ^b ^, ¹ , Weikang Mai ^a ^, ¹ , Daoyu Xia ^b ^, ¹ , Weidong Ding ^c , Xiaomian Zhou ^d , Min Deng ^a , Yu Lei ^a , Lu Chen ^a , Yantao Li ^b , Xiaorui Mai ^a , Lei Zhang ^e , Zheng Chen ^e , Yiru Qin ^f , Ruiwen Ren ^g , Wei Wei ^b ^, ^∗∗ , Tianxing Ji ^a ^, ^∗

Publication date (Electronic): 25 April 2023

Journal: Biosensors & Bioelectronics

Publisher: Published by Elsevier B.V.

Keywords: Lateral flow assay, Near-infrared, Downconversion nanoparticles, Neutralizing antibody, SARS-CoV-2, Ancestral strain, Omicron variants

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Abstract

Lateral flow assays (LFAs) are promising points-of-care tests, playing a vital role in diseases screening, diagnosis and surveillance. However, development of portable, cheap, and smart LFAs platform for sensitive and accurate quantification of disease biomarkers in complex media is challenging. Here, a cheap handheld device was developed to realize on-site detection of disease biomarkers by Nd ³⁺/Yb ³⁺ co-doped near-infrared (NIR)-to-NIR downconversion nanoparticles (DCNPs) based LFA. Its sensitivity is at least 8-fold higher for detecting NIR light signal from Nd ³⁺/Yb ³⁺ co-doped nanoparticles than conventional expensive InGaAs camera based detection platform. Additionally, we enhance NIR quantum yield of Nd ³⁺/Yb ³⁺ co-doped nanoparticles up to 35.5% via simultaneous high dopant of sensitizer ions Nd ³⁺ and emitter ions Yb ³⁺. Combination of NIR-to-NIR handheld detection device and ultra-bright NIR emitting NaNbF ₄:Yb60%@NaLuF ₄ nanoparticle probe allows the detection sensitivity of SARS-CoV-2 ancestral strain and Omicron variants specific neutralizing antibodies LFA up to the level of commercial enzyme linked immunosorbent assay kit. Furthermore, by this robust method, enhanced neutralizing antibodies against SARS-CoV-2 ancestral strain and Omicron variants are observed in healthy participants with Ad5-nCoV booster on top of two doses of inactivated vaccine. This NIR-to-NIR handheld platform provides a promising strategy for on-site evaluating protective humoral immunity after SARS-CoV-2 vaccination or infection.

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A SARS-CoV-2 surrogate virus neutralization test based on antibody-mediated blockage of ACE2–spike protein–protein interaction

Chee Wah Tan, Wan Ni Chia, Xijian Qin … (2020)

A robust serological test to detect neutralizing antibodies to SARS-CoV-2 is urgently needed to determine not only the infection rate, herd immunity and predicted humoral protection, but also vaccine efficacy during clinical trials and after large-scale vaccination. The current gold standard is the conventional virus neutralization test requiring live pathogen and a biosafety level 3 laboratory. Here, we report a SARS-CoV-2 surrogate virus neutralization test that detects total immunodominant neutralizing antibodies targeting the viral spike (S) protein receptor-binding domain in an isotype- and species-independent manner. Our simple and rapid test is based on antibody-mediated blockage of the interaction between the angiotensin-converting enzyme 2 (ACE2) receptor protein and the receptor-binding domain. The test, which has been validated with two cohorts of patients with COVID-19 in two different countries, achieves 99.93% specificity and 95-100% sensitivity, and differentiates antibody responses to several human coronaviruses. The surrogate virus neutralization test does not require biosafety level 3 containment, making it broadly accessible to the wider community for both research and clinical applications.

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BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection

Yunlong Cao, Ayijiang Yisimayi, Fanchong Jian … (2022)

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron sublineages BA.2.12.1, BA.4 and BA.5 exhibit higher transmissibility than the BA.2 lineage 1 . The receptor binding and immune-evasion capability of these recently emerged variants require immediate investigation. Here, coupled with structural comparisons of the spike proteins, we show that BA.2.12.1, BA.4 and BA.5 (BA.4 and BA.5 are hereafter referred collectively to as BA.4/BA.5) exhibit similar binding affinities to BA.2 for the angiotensin-converting enzyme 2 (ACE2) receptor. Of note, BA.2.12.1 and BA.4/BA.5 display increased evasion of neutralizing antibodies compared with BA.2 against plasma from triple-vaccinated individuals or from individuals who developed a BA.1 infection after vaccination. To delineate the underlying antibody-evasion mechanism, we determined the escape mutation profiles 2 , epitope distribution 3 and Omicron-neutralization efficiency of 1,640 neutralizing antibodies directed against the receptor-binding domain of the viral spike protein, including 614 antibodies isolated from people who had recovered from BA.1 infection. BA.1 infection after vaccination predominantly recalls humoral immune memory directed against ancestral (hereafter referred to as wild-type (WT)) SARS-CoV-2 spike protein. The resulting elicited antibodies could neutralize both WT SARS-CoV-2 and BA.1 and are enriched on epitopes on spike that do not bind ACE2. However, most of these cross-reactive neutralizing antibodies are evaded by spike mutants L452Q, L452R and F486V. BA.1 infection can also induce new clones of BA.1-specific antibodies that potently neutralize BA.1. Nevertheless, these neutralizing antibodies are largely evaded by BA.2 and BA.4/BA.5 owing to D405N and F486V mutations, and react weakly to pre-Omicron variants, exhibiting narrow neutralization breadths. The therapeutic neutralizing antibodies bebtelovimab 4 and cilgavimab 5 can effectively neutralize BA.2.12.1 and BA.4/BA.5, whereas the S371F, D405N and R408S mutations undermine most broadly sarbecovirus-neutralizing antibodies. Together, our results indicate that Omicron may evolve mutations to evade the humoral immunity elicited by BA.1 infection, suggesting that BA.1-derived vaccine boosters may not achieve broad-spectrum protection against new Omicron variants.

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Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5

Qian Wang, Yicheng Guo, Sho Iketani … (2022)

SARS-CoV-2 Omicron subvariants BA.2.12.1 and BA.4/5 have surged notably to become dominant in the United States and South Africa, respectively 1,2 . These new subvariants carrying further mutations in their spike proteins raise concerns that they may further evade neutralizing antibodies, thereby further compromising the efficacy of COVID-19 vaccines and therapeutic monoclonals. We now report findings from a systematic antigenic analysis of these surging Omicron subvariants. BA.2.12.1 is only modestly (1.8-fold) more resistant to sera from vaccinated and boosted individuals than BA.2. However, BA.4/5 is substantially (4.2-fold) more resistant and thus more likely to lead to vaccine breakthrough infections. Mutation at spike residue L452 found in both BA.2.12.1 and BA.4/5 facilitates escape from some antibodies directed to the so-called class 2 and 3 regions of the receptor-binding domain 3 . The F486V mutation found in BA.4/5 facilitates escape from certain class 1 and 2 antibodies but compromises the spike affinity for the viral receptor. The R493Q reversion mutation, however, restores receptor affinity and consequently the fitness of BA.4/5. Among therapeutic antibodies authorized for clinical use, only bebtelovimab retains full potency against both BA.2.12.1 and BA.4/5. The Omicron lineage of SARS-CoV-2 continues to evolve, successively yielding subvariants that are not only more transmissible but also more evasive to antibodies.

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Author and article information

Journal

Journal ID (nlm-ta): Biosens Bioelectron

Journal ID (iso-abbrev): Biosens Bioelectron

Title: Biosensors & Bioelectronics

Publisher: Published by Elsevier B.V.

ISSN (Print): 0956-5663

ISSN (Electronic): 1873-4235

Publication date PMC-release: 25 April 2023

Publication date (Electronic): 25 April 2023

Electronic Location Identifier: 115353

Affiliations

[a ]Clinical Laboratory Medicine Department, The Second Affiliated Hospital of Guangzhou Medical University, Guangzhou, 510260, PR China

[b ]MOE & Guangdong Provincial Key Laboratory of Laser Life Science, Guangzhou Key Laboratory of Spectral Analysis and Functional Probes, College of Biophotonics, South China Normal University, Guangzhou, 510631, PR China

[c ]Shenzhen Highcreation Technology Co., Ltd, Shenzhen, 518122, PR China

[d ]Guangzhou Biotron Technology Co, Ltd, Guangzhou, 510530, PR China

[e ]Kidney Transplant Department, The Second Affiliated Hospital of Guangzhou Medical University, 510260, PR China

[f ]Guangdong Provincial Key Laboratory of Occupational Disease Prevention and Treatment, Guangdong Province Hospital for Occupational Disease Prevention and Treatment, Guangzhou, 510300, PR China

[g ]Guangdong Arbovirus Diseases Emergency Technology Research Center, Guangzhou, 510507, PR China

Author notes

[∗ ]Corresponding author.

[∗∗ ]Corresponding author. MOE & Guangdong Provincial Key Laboratory of Laser Life Science, Guangzhou Key Laboratory of Spectral Analysis and Functional Probes, College of Biophotonics, South China Normal University, Guangzhou, PR China.

[1]

These authors contributed equally.

Article

Publisher Item ID: S0956-5663(23)00295-6 Publisher ID: 115353

DOI: 10.1016/j.bios.2023.115353

PMC ID: 10127741

PubMed ID: 37120945

SO-VID: 67b13625-70b9-44b3-8808-43ded063ef0f

License:

Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

History

Date received : 15 January 2023

Date revision received : 14 April 2023

Date accepted : 24 April 2023

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