2022
DOI: 10.1002/chem.202200523
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Front Cover: A Universal DNA Aptamer that Recognizes Spike Proteins of Diverse SARS‐CoV‐2 Variants of Concern (Chem. Eur. J. 15/2022)

Abstract: A unique DNA aptamer, denoted MSA52, displays universally high affinity for the spike proteins of the wild‐type SARS‐CoV‐2 as well as its Alpha, Beta, Gamma, Epsilon, Kappa, Delta and Omicron variants. This aptamer also recognizes pseudotyped lentiviruses expressing eight different spike proteins of SARS‐CoV‐2 with very high affinity, exhibiting dissociation constants (Kd) of 20–50 pM for these viruses. More information can be found in the Research Article by J. D. Brennan, Y. Li et al. (DOI: 10.1002/chem.2022… Show more

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Cited by 8 publications
(23 citation statements)
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“…[45][46][47] The existence of diverse VOCs poses another challenge for the development and utilization of S-protein binding aptamers because the associated mutations could negatively impact the affinity of the aptamers derived using the spike protein from the original SARS-CoV-2 virus. However, with the exception of our universal aptamer MSA52 that exhibited universally high affinity binding to spike proteins from eight VOCs, [48] only a few other aptamers have been tested for binding to the S-protein variants, and in these cases only one or two VOCs were tested. [27,28,30] Further testing with more S-proteins variants is necessary to determine the performance of these aptamers for VOC recognition.…”
Section: Introductionmentioning
confidence: 99%
“…[45][46][47] The existence of diverse VOCs poses another challenge for the development and utilization of S-protein binding aptamers because the associated mutations could negatively impact the affinity of the aptamers derived using the spike protein from the original SARS-CoV-2 virus. However, with the exception of our universal aptamer MSA52 that exhibited universally high affinity binding to spike proteins from eight VOCs, [48] only a few other aptamers have been tested for binding to the S-protein variants, and in these cases only one or two VOCs were tested. [27,28,30] Further testing with more S-proteins variants is necessary to determine the performance of these aptamers for VOC recognition.…”
Section: Introductionmentioning
confidence: 99%
“…Zhang et al completed 13 selection rounds with wild-type SARS-CoV-2 S1, but then conducted ve separate selection rounds using different variants of SARS-CoV-2 S protein. 57 Another issue with protein-SELEX is that typically embedded or inward-facing portions of membrane proteins can be exposed during selection, potentially allowing aptamers to bind to an inaccessible location in the native state. One strategy to avoid this issue is to conduct selection with enveloped viruses.…”
Section: Selection Targetsmentioning
confidence: 99%
“…Before modern methods, radioactive isotopes were used to label aptamers, but now, many SELEX protocols use uorescently labeled primers. Apparent K D binding can be measured by methods like cell ow cytometry, 56,66 dot blot assay, 57 and direct ELISAs. 56,76 Techniques that directly measure binding kinetics include surface plasmon resonance (SPR) 32,77 and biolayer interferometry (BLI).…”
Section: Improving and Evaluating Library Bindingmentioning
confidence: 99%
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“…To address this issue, we recently made an effort to select for universal DNA aptamers that recognize several VoCs. [87] Our previous DNA aptamers, mainly MSA1 and MSA5, were targeted specifically to the S1 subunit of the wildtype spike protein. However, it was realized that the epitopes recognized by these two aptamers were sensitive to the changes caused by the mutations to the S protein.…”
Section: Aptamer Binding To Variants Of Concernmentioning
confidence: 99%