From Ugly Duckling to Swan: Unexpected Identification from Cell-SELEX of an Anti-Annexin A2 Aptamer Targeting Tumors

Cibiel, Agnès; Quang, Nam Nguyen; Gombert, Karine; Thézé, Benoît; Garofalakis, Anikitos; Ducongé, Frédéric

doi:10.1371/journal.pone.0087002

Cited by 36 publications

(33 citation statements)

References 51 publications

(56 reference statements)

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“…Cells were incubated at 37°C for 45 min with the aptamer sequences A26 and A33 that were found to be highly specific toward MCF7 cells, [8] and with A33sc (scrambled sequence) characterized by the lack of specificity to the studied cells ( Table 1). Stock solutions (25 mm in DPBS buffer) of the oligonucleotide sequences were incubated at 90°C for 5 min, and then cooled down to room temperature by the natural cooling process to the 37°C facilitating the proper 3D structures of aptamers during renaturation.…”

Section: Aptamers Binding Assaymentioning

confidence: 99%

“…[8] This membrane-bound protein that is involved in heat stress response, angiogenesis, cell proliferation, and adhesion may cross the membrane as a constituent of the lipid raft assembly; however, it has not been described to occur in the glycosylated form. [8] This membrane-bound protein that is involved in heat stress response, angiogenesis, cell proliferation, and adhesion may cross the membrane as a constituent of the lipid raft assembly; however, it has not been described to occur in the glycosylated form.…”

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confidence: 99%

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Changes in Protein Glycosylation as a Result of Aptamer Interactions with Cancer Cells

Drabik

Ner‐Kluza

Hartman

et al. 2019

Proteomics Clinical Apps

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Purpose Based on the recent aptamer‐related breast cancer studies, which indicate the therapeutic role of specific oligonucleotide sequences, experiments have been designed in an attempt to unravel the molecular targets of this mechanism. This article describes the study on glycoproteome changes in breast cancer cells as a result of their interactions with aptamers. Experimental design Aberrations in protein glycosylation play an important role in tumorigenesis and influence cancer progression, metastasis, immunoresponse, and chemoresistance, therefore this study is focused on the identification of the alterations in glycan expression on the surface of proteins as a potential and innovative tool for biomedical applications of aptamers in cancer treatment. Results Two proteins, kinesin‐like protein (KI13B) and proliferating cell nuclear antigen (PCNA), have been identified that carry N‐glycan epitopes after conjugation with aptamer sequences. Conclusions and clinical relevance Multiple features of aptamers as an alternative to protein antibodies are utilized for various biomedical applications ranging from biomarker discovery, bioimaging, targeted therapy, drug delivery, and drug pharmacokinetics and biodistribution. Frequently, aptamers bind to their target molecules and modulate their function. Such therapeutic aptamers can modify the biological pathways for treatment of many types of diseases, such as cancer.

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Section: Aptamers Binding Assaymentioning

confidence: 99%

mentioning

confidence: 99%

Changes in Protein Glycosylation as a Result of Aptamer Interactions with Cancer Cells

Drabik

Ner‐Kluza

Hartman

et al. 2019

Proteomics Clinical Apps

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“…These technologies have already been reviewed [7,9,10]. In most cases, “adapter” sequences have to be linked at the extremity of sequences by ligation or PCR amplification [11,12,13]. These adapters will be used to amplify the sequences and attach them to a sequencing support before sequencing (Flowcell, beads...).…”

Section: Preparation Of Libraries For Htsmentioning

confidence: 99%

“…Thus, it seems that sequences could be amplified during SELEX based on other criteria than binding for the expected target. Such unwanted selection was also observed in a cell-SELEX against CHO-K1 cells overexpressing endothelin type B receptor [11]. The wild type CHO-K1 cell line was used at every round in negative selection steps to discard any aptamer that could be selected against other membrane proteins than ETBR.…”

Section: Study Of Evolutionmentioning

confidence: 99%

Applications of High-Throughput Sequencing for In Vitro Selection and Characterization of Aptamers

2016

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Aptamers are identified through an iterative process of evolutionary selection starting from a random pool containing billions of sequences. Simultaneously to the amplification of high-affinity candidates, the diversity in the pool is exponentially reduced after several rounds of in vitro selection. Until now, cloning and Sanger sequencing of about 100 sequences was usually used to identify the enriched candidates. However, High-Throughput Sequencing (HTS) is now extensively used to replace such low throughput sequencing approaches. Providing a deeper analysis of the library, HTS is expected to accelerate the identification of aptamers as well as to identify aptamers with higher affinity. It is also expected that it can provide important information on the binding site of the aptamers. Nevertheless, HTS requires handling a large amount of data that is only possible through the development of new in silico methods. Here, this review presents these different strategies that have been recently developed to improve the identification and characterization of aptamers using HTS.

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“…However, despite negative selection steps using mock (negative-control) cells, this method sometimes results in aptamers against undesirable targets that are expressed both on mock and targeted cells. In an interesting study, the researchers suggested that it was possible to pull viable candidates from these “junk” aptamers for different applications from those originally envisaged [44]. Aptamers identification was originally performed against CHO-K1 cells expressing human Endothelin type B receptor (ETBR) using CHO-K1 cells as the control.…”

Section: Fluorescence Imaging With Aptamersmentioning

confidence: 99%

Applications of Aptamers in Targeted Imaging: State of the Art

Dougherty¹,

Cai

Hong³

2015

CTMC

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Aptamers are single-stranded oligonucleotides with high affinity and specificity to the target molecules or cells, thus they can serve as an important category of molecular targeting ligand. Since their discove1y, aptamers have been rapidly translated into clinical practice. The strong target affinity/selectivity, cost-effectivity, chemical versatility and safety of aptamers are superior to traditional peptides- or proteins-based ligands which make them unique choices for molecular imaging. Therefore, aptamers are considered to be extremely useful to guide various imaging contrast agents to the target tissues or cells for optical, magnetic resonance, nuclear, computed tomography, ultra sound and multimodality imaging. This review aims to provide an overview of aptamers' advantages as targeting ligands and their application in targeted imaging. Further research in synthesis of new types of aptamers and their conjugation with new categories of contrast agents is required to develop clinically translatable aptamer-based imaging agents which will eventually result in improved patient care.

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From Ugly Duckling to Swan: Unexpected Identification from Cell-SELEX of an Anti-Annexin A2 Aptamer Targeting Tumors

Cited by 36 publications

References 51 publications

Changes in Protein Glycosylation as a Result of Aptamer Interactions with Cancer Cells

Changes in Protein Glycosylation as a Result of Aptamer Interactions with Cancer Cells

Applications of High-Throughput Sequencing for In Vitro Selection and Characterization of Aptamers

Applications of Aptamers in Targeted Imaging: State of the Art

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