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Review
. 2024 Feb 13;14(2):99.
doi: 10.3390/bios14020099.

Unraveling the Dynamics of SARS-CoV-2 Mutations: Insights from Surface Plasmon Resonance Biosensor Kinetics

Devi Taufiq Nurrohman  1 , Nan-Fu Chiu  1   2
Affiliations
Review

Unraveling the Dynamics of SARS-CoV-2 Mutations: Insights from Surface Plasmon Resonance Biosensor Kinetics

Devi Taufiq Nurrohman et al. Biosensors (Basel). .

Abstract

Surface Plasmon Resonance (SPR) technology is known to be a powerful tool for studying biomolecular interactions because it offers real-time and label-free multiparameter analysis with high sensitivity. This article summarizes the results that have been obtained from the use of SPR technology in studying the dynamics of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mutations. This paper will begin by introducing the working principle of SPR and the kinetic parameters of the sensorgram, which include the association rate constant (ka), dissociation rate constant (kd), equilibrium association constant (KA), and equilibrium dissociation constant (KD). At the end of the paper, we will summarize the kinetic data on the interaction between angiotensin-converting enzyme 2 (ACE2) and SARS-CoV-2 obtained from the results of SPR signal analysis. ACE2 is a material that mediates virus entry. Therefore, understanding the kinetic changes between ACE2 and SARS-CoV-2 caused by the mutation will provide beneficial information for drug discovery, vaccine development, and other therapeutic purposes.

Keywords: COVID-19; biosensors; kinetics; surface plasmon resonance.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Schematic diagram to illustrate the contents of this paper.
Figure 2
Figure 2
(a) Surface plasmon dispersion curve. (b) Schematic of the prism-coupled SPR biosensor and the resulting signal.
Figure 3
Figure 3
(a) Biosensor chip architecture; (b) SPR sensorgram at different phase.
Figure 4
Figure 4
Structure of the SARS-CoV-2 virus. Reproduced with permission from [45]. Copyright (2023), Springer.
Figure 5
Figure 5
3D structure of the spike protein of SARS-CoV-2 variants alpha, beta, gamma, delta, and omicron in comparison with an ancestral virus. Reproduced with permission from [50]. Copyright (2023), mBio.
Figure 6
Figure 6
SPR sensorgram showing kinetic binding for ACE2 with (a) 2019-nCoV S, (b) SARS-CoV RBD-SD1. Reproduced with permission from [67]. Copyright (2020), Science.
Figure 7
Figure 7
Binding curves of immobilized human ACE2 with the SARS-CoV-2 RBD (a) and SARS-CoV RBD (b). Reproduced with permission from [43]. Copyright (2020), Nature.
Figure 8
Figure 8
Kinetic parameters (ka, kd, and KD) due to (a) RBD mutation and (b) ACE2 mutation. Reproduced with permission from [71]. Copyright (2020), eLife.
See this image and copyright information in PMC

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