Cell surface-engineering to embed targeting ligands or tracking agents on the cell membrane

Lim, Kyutae; Lee, Daniel Y.; Valencia, Gabriel M.; Won, Young‐Wook; Bull, David A.

doi:10.1016/j.bbrc.2016.11.155

Cited by 15 publications

(17 citation statements)

References 32 publications

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“…These results are consistent with those obtained by others performing similar hydrophobic insertions and further validates this approach as a universal method for cell surface modification. 3, 4, 18, 34–37…”

Section: Resultsmentioning

confidence: 99%

Engineering Reversible Cell–Cell Interactions with Lipid Anchored Prosthetic Receptors

et al. 2018

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Membrane-engineered cells displaying antigen-targeting ligands are useful as both scientific tools and clinical therapeutics. While genetically encoded artificial receptors have proven efficacious, their scope remains limited, as this approach is not amenable to all cell types and the modification is often permanent. Our group has developed a nongenetic method to rapidly, stably, and reversibly modify any cell membrane with a chemically self-assembled nanoring (CSAN) that can function as a prosthetic receptor. Bifunctional CSANs displaying epithelial cell adhesion molecule (EpCAM)-targeted fibronectin domains were installed on the cell membrane through hydrophobic insertion and remained stably bound for ≥72 h in vitro. These CSAN-labeled cells were capable of recognizing EpCAM-expressing target cells, forming intercellular interactions that were subsequently reversed by disassembling the nanoring with the FDA-approved antibiotic, trimethoprim. This study demonstrates the use of this system to engineer cell surfaces with prosthetic receptors capable of directing specific and reversible cell-cell interactions.

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Section: Resultsmentioning

confidence: 99%

Engineering Reversible Cell–Cell Interactions with Lipid Anchored Prosthetic Receptors

et al. 2018

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“…Lim, K.S., et al also studied DMPE-PEG-peptide conjugates on MSCs to promote adhesion between the CRPPR peptide and the CRIP2 protein receptor. Jurkat cells were also modified with DMPE-PEG-SPION-FITC to show cells could be modified with tracking agents [110].…”

Section: Coatings Designmentioning

confidence: 99%

Coatings on mammalian cells: interfacing cells with their environment

Davis

Cahall

et al. 2019

J Biol Eng

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The research community is intent on harnessing increasingly complex biological building blocks. At present, cells represent a highly functional component for integration into higher order systems. In this review, we discuss the current application space for cellular coating technologies and emphasize the relationship between the target application and coating design. We also discuss how the cell and the coating interact in common analytical techniques, and where caution must be exercised in the interpretation of results. Finally, we look ahead at emerging application areas that are ideal for innovation in cellular coatings. In all, cellular coatings leverage the machinery unique to specific cell types, and the opportunities derived from these hybrid assemblies have yet to be fully realized.

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“…In recent years, using purified protein or whole virus particle as the targets of phage peptide library screening provides an ideal approach to identify multifunctional peptides [22,[34][35][36]. In this study, we used a phage-displayed heptapeptide library to identify G 1 protein interactors, and the conditions of the selection were strictly limited to enrichment specific G 1 -binding phages( Table 2).…”

Section: Discussionmentioning

confidence: 99%

Biopanning of polypeptides binding to bovine ephemeral fever virus G1 protein from phage display peptide library

Hou

Zhao

et al. 2018

BMC Vet Res

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BackgroundThe bovine ephemeral fever virus (BEFV) glycoprotein neutralization site 1 (also referred as G1 protein), is a critical protein responsible for virus infectivity and eliciting immune-protection, however, binding peptides of BEFV G1 protein are still unclear. Thus, the aim of the present study was to screen specific polypeptides, which bind BEFV G1 protein with high-affinity and inhibit BEFV replication.MethodsThe purified BEFV G1 was coated and then reacted with the M13-based Ph.D.-7 phage random display library. The peptides for target binding were automated sequenced after four rounds of enrichment biopanning. The amino acid sequences of polypeptide displayed on positive clones were deduced and the affinity of positive polypeptides with BEFV G1 was assayed by ELISA. Then the roles of specific G1-binding peptides in the context of BEFV infection were analyzed.ResultsThe results showed that 27 specific peptide ligands displaying 11 different amino acid sequences were obtained, and the T18 and T25 clone had a higher affinity to G1 protein than the other clones. Then their antiviral roles of two phage clones (T25 and T18) showed that both phage polypeptide T25 and T18 exerted inhibition on BEFV replication compared to control group. Moreover, synthetic peptide based on T18 (HSIRYDF) and T25 (YSLRSDY) alone or combined use on BEFV replication showed that the synthetic peptides could effectively inhibit the formation of cytopathic plaque and significantly inhibit BEFV RNA replication in a dose-dependent manner.ConclusionTwo antiviral peptide ligands binding to bovine ephemeral fever virus G1 protein from phage display peptide library were identified, which may provide a potential research tool for diagnostic reagents and novel antiviral agents.Electronic supplementary materialThe online version of this article (10.1186/s12917-017-1315-x) contains supplementary material, which is available to authorized users.

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Cell surface-engineering to embed targeting ligands or tracking agents on the cell membrane

Cited by 15 publications

References 32 publications

Engineering Reversible Cell–Cell Interactions with Lipid Anchored Prosthetic Receptors

Engineering Reversible Cell–Cell Interactions with Lipid Anchored Prosthetic Receptors

Coatings on mammalian cells: interfacing cells with their environment

Biopanning of polypeptides binding to bovine ephemeral fever virus G1 protein from phage display peptide library

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