Structurally Different Yet Functionally Similar: Aptamers Specific for the Ebola Virus Soluble Glycoprotein and GP1,2 and Their Application in Electrochemical Sensing

Soma Banerjee; Mahsa Askary Hemmat; Shambhavi Shubham; Agnivo Gosai; Sivaranjani Devarakonda; Nianyu Jiang; Charith Geekiyanage; Jacob A Dillard; Wendy Maury; Pranav Shrotriya; Monica H Lamm; Marit Nilsen-Hamilton

doi:10.3390/ijms24054627

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Structurally Different Yet Functionally Similar: Aptamers Specific for the Ebola Virus Soluble Glycoprotein and GP1,2 and Their Application in Electrochemical Sensing

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Structurally Different Yet Functionally Similar: Aptamers Specific for the Ebola Virus Soluble Glycoprotein and GP1,2 and Their Application in Electrochemical Sensing

Soma Banerjee, Mahsa Askary Hemmat, Shambhavi Shubham, Agnivo Gosai, Sivaranjani Devarakonda, Nianyu Jiang, Charith Geekiyanage, Jacob A Dillard, Wendy Maury, Pranav Shrotriya, …

International journal of molecular sciences, Vol.24(5), 4627

03/01/2023

DOI: 10.3390/ijms24054627

PMCID: PMC10003157

PMID: 36902059

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Abstract

The Ebola virus glycoprotein (GP) gene templates several mRNAs that produce either the virion-associated transmembrane protein or one of two secreted glycoproteins. Soluble glycoprotein (sGP) is the predominant product. GP1 and sGP share an amino terminal sequence of 295 amino acids but differ in quaternary structure, with GP1 being a heterohexamer with GP2 and sGP a homodimer. Two structurally different DNA aptamers were selected against sGP that also bound GP1,2. These DNA aptamers were compared with a 2'FY-RNA aptamer for their interactions with the Ebola GP gene products. The three aptamers have almost identical binding isotherms for sGP and GP1,2 in solution and on the virion. They demonstrated high affinity and selectivity for sGP and GP1,2. Furthermore, one aptamer, used as a sensing element in an electrochemical format, detected GP1,2 on pseudotyped virions and sGP with high sensitivity in the presence of serum, including from an Ebola-virus-infected monkey. Our results suggest that the aptamers interact with sGP across the interface between the monomers, which is different from the sites on the protein bound by most antibodies. The remarkable similarity in functional features of three structurally distinct aptamers suggests that aptamers, like antibodies, have preferred binding sites on proteins.

Ebola sGP

aptamer–protein interaction

electrochemical sensor

Ebola GP1,2

aptamers

Details

Title: Subtitle: Structurally Different Yet Functionally Similar: Aptamers Specific for the Ebola Virus Soluble Glycoprotein and GP1,2 and Their Application in Electrochemical Sensing
Creators: Soma Banerjee - Ames National Laboratory
Mahsa Askary Hemmat - Iowa State University
Shambhavi Shubham - Iowa State University
Agnivo Gosai - Iowa State University
Sivaranjani Devarakonda - Iowa State University
Nianyu Jiang - Iowa State University
Charith Geekiyanage
Jacob A Dillard - University of Iowa
Wendy Maury - University of Iowa
Pranav Shrotriya - Iowa State University
Monica H Lamm - Iowa State University
Marit Nilsen-Hamilton - Iowa State University
Resource Type: Journal article
Publication Details: International journal of molecular sciences, Vol.24(5), 4627
DOI: 10.3390/ijms24054627
PMID: 36902059
PMCID: PMC10003157
NLM abbreviation: Int J Mol Sci
ISSN: 1661-6596
eISSN: 1422-0067
Grant note: R01AI077519 / NIH HHS none / Aptalogic Inc. R43AI118139 / National Institute of Health R01AI134733 / NIH HHS
Language: English
Date published: 03/01/2023
Academic Unit: Microbiology and Immunology
Record Identifier: 9984375448802771

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