Chaperonin GroEL a Brucella immunodominant antigen identified using Nanobody and MALDI-TOF-MS technologies

Abbady, Abdul Qader; Al-Daoude, A.; Al-Mariri, Ayman; Zarkawi, M.; Muyldermans, Serge

doi:10.1016/j.vetimm.2012.01.015

Cited by 28 publications

(17 citation statements)

References 46 publications

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“…Therefore, recombinant GroEL proteins of some species have been expressed to verify their immunogenicity [28,45,46]. Recently, Abbady et al confirmed GroEL as an immunodominant antigen of Brucella by Nanobody and MALDI-TOF-MS technologies [36]. Nevertheless, prior to this study, the immunogenicity of APEC GroEL had not been reported.…”

Section: Discussionmentioning

confidence: 85%

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Chaperonin GroEL: A novel phylogenetically conserved protein with strong immunoreactivity of Avian Pathogenic Escherichia coli isolates from duck identified by immunoproteomics

Bao

Zhai

Wang

et al. 2013

Vaccine

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Section: Discussionmentioning

confidence: 85%

“…The other nine proteins of APEC exhibiting immunoreactivity were previously unidentified. Among these, GroEL, AtpD, MalE, Tsf and Pnp have been shown to be immunogenic in other species [36][37][38][39].…”

Section: Discussionmentioning

confidence: 99%

Chaperonin GroEL: A novel phylogenetically conserved protein with strong immunoreactivity of Avian Pathogenic Escherichia coli isolates from duck identified by immunoproteomics

Bao

Zhai

Wang

et al. 2013

Vaccine

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“…Diagnostic and therapeutic [143] HER2 Breast cancer Diagnostic [144,145] HPV-16 L1 protein Cervical cancer Diagnostic and therapeutic [146,147] HSP-60 Brucellosis (livestock) Diagnostic and vaccine [23,148] VCAM1 Atherosclerotic lesions Molecular imaging [149][150][151] VEGFR2 Angiogenesis Therapeutic [152] TNT Explosive Diagnostic [133,153] SEB Toxin Sensor and diagnostic [134] Ricin Toxin Sensor and diagnostic [134] BoNT/A Toxin Sensor and diagnostic [90,154,155] Scorpion AahII Toxin Neutralizing and therapeutic [135] EGFR binding reagents, derived from conventional polyclonal sera, monoclonal antibodies, small fragments (Fab and scFv) and peptides [145]. Foley and co-workers demonstrated the heat stability of purified recombinant V NAR was superior to that of conventional mAbs by targeting immobilized P. falciparum AMA1 in various formats at 45°C, and the refolding property of V NAR was retained when the temperature increased to 80°C.…”

Section: Vegf-a 165 Neoangiogenesismentioning

confidence: 99%

The Development of Single Domain Antibodies for Diagnostic and Therapeutic Applications

Leow¹,

Cheng²,

Fischer³

et al. 2018

Antibody Engineering

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Monoclonal antibodies have become increasingly accepted as diagnostics and therapeutics for various human diseases due to their high affinity and specificity. However, several practical drawbacks are apparent for the reagents based on conventional IgG antibodies. With the emergence of antibody engineering, many problems were overcome when the recombinant antibody fragments such as Fabs, scFvs, diabodies and single domain antibodies (sdAbs), are developed. These fragments not only retain the specificity of the whole monoclonal antibodies, but are also easy to express and produce in prokaryotic expression systems. Rather unexpectedly, the natural sdAbs namely V HH s, V NAR s and variable lymphocyte receptors (VLRs) that comprise excellent biological activities were recently discovered in camelids, cartilaginous fish and lampreys, respectively. Due to their unique characteristics, including small size, high thermostability, stable folding in the nucleus and cytosol and long CDR3 regions which have access to cavities or clefts on the surface of proteins, these new binders are now investigated extensively as a substitute for conventional antibodies. This review describes the potential of sdAbs selected using in vitro display systems and their use in multiple applications.(polyclonal Abs) are heterogeneous antibody mixtures that are derived from multiple plasma cell lines. Because polyclonal antibodies comprise a mixture of different antibodies carrying numerous paratopes, they have excellent properties for recognizing antigens [2]. A monoclonal antibody (mAb) is a homogeneous antibody generated from a single B lymphocyte clone. Antibodies produced in mAb format have an extremely high specificity against a single epitope on antigens [3]. Recombinant antibodies (rAbs) are antibodies generated using molecular biology techniques. They are aimed to improve the sensitivity, selectivity, stability and immobilization properties in diagnostic applications, for example, in biosensors [4]. In making decision to use or generate polyclonal, monoclonal or recombinant antibodies, several factors should be considered, including commercial availability, possibility to raise animals, types of applications, time length of a project and costs [1]. Although a vast number of rAbs has been proposed [5][6][7][8], the natural sdAb fragments that were recently discovered from camelids (V HH s), sharks (V NAR s) and lampreys (VLRs) have shown to possess extraordinary features that are not found in conventional antibodies, such as a small dimension, an elevated stability and the capability of recognizing cavities and clefts on the surface of proteins that cannot be reached by conventional recombinant antibodies [9][10][11]. This chapter will discuss the availability of new binders derived from vertebrates and give an overview of their applications in a biomedical platform by recognizing specified targets from various diseases. Monoclonal antibodies and their limitationsThe first description of monoclonal antibody (mAbs) production was published ...

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“…Human epidermal growth factor receptor (HER) 2‐Nbs were used as probes in positron emission tomography (PET)/computer tomography (CT) imaging of breast carcinoma patients . The high binding capacity of Nbs results in high sensitivity combined with high specificity . The relatively short half‐life, tumour penetration ability and fast extravasation lead to low background noise .…”

Section: Antibody‐based Ligand Scaffoldmentioning

confidence: 99%

A current perspective on applications of macrocyclic‐peptide‐based high‐affinity ligands

2016

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Monoclonal antibodies can bind with high affinity and high selectivity to their targets. As a tool in therapeutics or diagnostics, however, their large size (∼150 kDa) reduces penetration into tissue and prevents passive cellular uptake. To overcome these and other problems, minimized protein scaffolds have been chosen or engineered, with care taken to not compromise binding affinity or specificity. An alternate approach is to begin with a minimal non‐antibody scaffold and select functional ligands from a de novo library. We will discuss the structure, production, applications, strengths, and weaknesses of several classes of antibody‐derived ligands, that is, antibodies, intrabodies, and nanobodies, and nonantibody‐derived ligands, that is, monobodies, affibodies, and macrocyclic peptides. In particular, this review is focussed on macrocyclic peptides produced by the Random non‐standard Peptides Integrated Discovery (RaPID) system that are small in size (typically ∼2 kDa), but are able to perform tasks typically handled by larger proteinaceous ligands.

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Chaperonin GroEL a Brucella immunodominant antigen identified using Nanobody and MALDI-TOF-MS technologies

Cited by 28 publications

References 46 publications

Chaperonin GroEL: A novel phylogenetically conserved protein with strong immunoreactivity of Avian Pathogenic Escherichia coli isolates from duck identified by immunoproteomics

Chaperonin GroEL: A novel phylogenetically conserved protein with strong immunoreactivity of Avian Pathogenic Escherichia coli isolates from duck identified by immunoproteomics

The Development of Single Domain Antibodies for Diagnostic and Therapeutic Applications

A current perspective on applications of macrocyclic‐peptide‐based high‐affinity ligands

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