Array-based analysis of SARS-CoV-2, other coronaviruses, and influenza antibodies in convalescent COVID-19 patients

Steiner, Daniel J.; Cognetti, John S.; Luta, Ethan P.; Klose, Alanna; Bucukovski, Joseph; Bryan, Michael; Schmuke, Jon J.; Nguyen-Contant, Phuong; Sangster, Mark Y.; Topham, David J.; Miller, Benjamin L.

doi:10.1016/j.bios.2020.112643

Cited by 35 publications

(40 citation statements)

References 24 publications

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“…The Middle East respiratory syndrome CoV (MERS-CoV) RBD was from Sino Biological (catalog 40071-V08B1; Wayne, PA). It is a recombinant C-terminal His-tagged protein consisting of Glu367-Tyr606 of MERS-CoV S protein (GenBank accession: AFS88936.1) (23). The purity of the protein was >90%, as determined by SDS-PAGE.…”

Section: Protein Constructsmentioning

confidence: 99%

Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction

Cao¹,

Dong²,

Kim

et al. 2021

Biophysical Journal

100

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The current COVID-19 pandemic has led to a devastating impact across the world. SARS-CoV-2 (the virus causing COVID-19) is known to use the receptor-binding domain (RBD) at viral surface spike (S) protein to interact with the angiotensin-converting enzyme 2 (ACE2) receptor expressed on many human cell types. The RBD−ACE2 interaction is a crucial step to mediate the host cell entry of SARS-CoV-2. Recent studies indicate that the ACE2 interaction with the SARS-CoV-2 S protein has a higher affinity than its binding with the structurally identical S protein of SARS-CoV-1, the virus causing the 2002-2004 SARS outbreak. However, the biophysical mechanism behind such binding affinity difference is unclear. This study utilizes combined single-molecule force spectroscopy and steered molecular dynamics (SMD) simulation approaches to quantify the specific interactions between CoV-2 or CoV-1 RBD and ACE2. Depending on the loading rates, the unbinding forces between CoV-2 RBD and ACE2 range from 70 to 105 pN and are 30-40% higher than those of CoV-1 RBD and ACE2 under similar loading rates. SMD results indicate that CoV-2 RBD interacts with the N-linked glycan on Asn90 of ACE2. This interaction is mostly absent in the CoV-1 RBD−ACE2 complex. During the SMD simulations, the extra RBD-N-glycan interaction contributes to a greater force and prolonged interaction lifetime. The observation is confirmed by our experimental force spectroscopy study. After removing N-linked glycans on ACE2, its mechanical binding strength with CoV-2 RBD decreases to a similar level of the CoV-1 RBD−ACE2 interaction. Together, the study uncovers the mechanism behind the difference in ACE2 binding between SARS-CoV-2 and SARS-CoV-1 and could help develop new strategies to block SARS-CoV-2 entry.

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Section: Protein Constructsmentioning

confidence: 99%

Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction

Cao¹,

Dong²,

Kim

et al. 2021

Biophysical Journal

100

View full text Add to dashboard Cite

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“…These monobodies can be also coated on the magnetic beads to pull down and enrich SARS-CoV-2 virus particles from patient nasal swab samples for RT-PCR. In addition, human immunoglobulins, e.g., IgG or IgM can be quantitatively detected by a multiplex label-free antigen microarray on the Arrayed Imaging Reflectometry (AIR) platform [ 83 ].…”

Section: Recent Biosensing Approaches For Detecting Sars-cov-2mentioning

confidence: 99%

Advances in emergent biological recognition elements and bioelectronics for diagnosing COVID-19

et al. 2021

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Coronaviruses pose a serious threat to public health. Tremendous efforts are dedicated to advance reliable and effective detection of coronaviruses. Currently, the coronavirus disease 2019 (COVID-19) diagnosis mainly relies on the detection of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genetic materials by using reverse transcription-polymerase chain reaction (RT-PCR) assay. However, simpler and more rapid and reliable alternatives are needed to meet high demand during the pandemic. Biosensor-based diagnosis approaches become alternatives for selectively and rapidly detecting virus particles because of their biorecognition elements consisting of biomaterials that are specific to virus biomarkers. Here, we summarize biorecognition materials, including antibodies and antibody-like molecules, that are designed to recognize SARS-CoV-2 biomarkers and the advances of recently developed biosensors for COVID-19 diagnosis. The design of biorecognition materials or layers is crucial to maximize biosensing performances, such as high selectivity and sensitivity of virus detection. Additionally, the recent representative achievements in developing bioelectronics for sensing coronavirus are included. This review includes scholarly articles, mainly published in 2020 and early 2021. In addition to capturing the fast development in the fields of applied materials and biodiagnosis, the outlook of this rapidly evolving technology is summarized. Early diagnosis of COVID-19 could help prevent the spread of this contagious disease and provide significant information to medical teams to treat patients.

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“…Multiplexed testing enables detection of immunoglobulin binding to more than one antigen within a single tube, well, plate or slide. These include, but are not limited to MIAs such as Luminex-based assays (Ayouba et al 2020; Randad et al 2020), fluorescent protein microarrays (Hedde et al 2020), and direct/label-free array technologies (Steiner et al 2020). The key challenges with these approaches are achieving high sensitivity, and low rate of false positives (selectivity), and quantitative measurement of immunoglobulin concentration/titer across a large dynamic range.…”

Section: Introductionmentioning

confidence: 99%

Multiplexed Detection and Quantification of Human Antibody Response to COVID-19 Infection Using a Plasmon Enhanced Biosensor Platform

Cady

Tokranova

Minor

et al. 2020

Preprint

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The 2019 SARS CoV-2 (COVID-19) pandemic has highlighted the need for rapid and accurate tests to diagnose acute infection and immune response to infection. A multiplexed assay built on grating-coupled fluorescent plasmonics (GC-FP) was shown to have 100% selectivity and sensitivity (n = 23) when measuring serum IgG levels against three COVID-19 antigens (spike S1, spike S1S2, and the nucleocapsid protein). The entire assay takes less than 30 min, making it highly competitive with well-established ELISA and immunofluorescence assays. GC-FP is quantitative over a large dynamic range, providing a linear response for serum titers ranging from 1:25 to 1:1,600, and shows high correlation with both ELISA and a Luminex-based microsphere immunoassay (MIA) (Pearson r > 0.9). Compatibility testing with dried blood spot samples (n = 63) demonstrated 100% selectivity and 86.7% sensitivity. A machine learning (ML) model was trained to classify dried blood spot samples for prior COVID-19 infection status, based on the combined antibody response to S1, S1S2, and Nuc antigens. The ML model yielded 100% selectivity and 80% sensitivity and demonstrated a higher stringency than diagnosis with a single antibody-antigen response. The platform is flexible and will readily accommodate IgG, IgM, and IgA. Further, the assay uses sub-nanogram quantities of capture ligand and is thus readily modified to include additional antigens, which is shown by the addition of RBD in later iterations of the test. The combination of rapid, multiplexed, and quantitative detection for both blood serum and dried blood spot samples makes GC-FP an attractive approach for COVID-19 antibody testing.

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Array-based analysis of SARS-CoV-2, other coronaviruses, and influenza antibodies in convalescent COVID-19 patients

Cited by 35 publications

References 24 publications

Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction

Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction

Advances in emergent biological recognition elements and bioelectronics for diagnosing COVID-19

Multiplexed Detection and Quantification of Human Antibody Response to COVID-19 Infection Using a Plasmon Enhanced Biosensor Platform

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