Abstract
Antibodies have different chemical properties capable of targeting a diverse nature of antigens. Traditionally, immune antibody libraries are perceived to be disease-specific with a skewed repertoire. The complexity during the generation of a combinatorial antibody library allows for a skewed but diverse repertoire to be generated. Strongyloides stercoralis is a parasite that causes strongyloidiasis, a potentially life-threatening disease with a complex diagnosis that impedes effective control and treatment of the disease. This study describes the isolation of monoclonal antibodies against S. stercoralis NIE recombinant protein using an immune antibody phage display library derived from lymphatic filaria-infected individuals. The isolated antibody clones showed both lambda and kappa light chains gene usage, with diverse amino acid distributions. Structural analysis showed that electropositivity and the interface area could determine the binding affinity of the clones with NIE. The successful identification of S. stercoralis antibodies from the filarial immune library highlights the breadth of antibody gene diversification in an immune antibody library that can be applied for closely related infections.
Highlights
In the past decade, phage display technology has become a common tool for the discovery of novel binders against various antigen targets[1]
The antibody repertoire in immune libraries consists of B cells that have been exposed to a particular pathogen and have undergone affinity maturation processes[2]
The analysis showed the rNIE was produced with good yield and purity suitable for biopanning
Summary
Phage display technology has become a common tool for the discovery of novel binders against various antigen targets[1]. The drawback of naïve library-derived antibodies is a general lower affinity compared to antibodies from an immune source and a higher possibility of cross-reactions[4,5] This limitation may be circumvented by in vitro affinity maturation processes. We utilized a previously constructed Human AntibodY Disease ENhanced (HAYDEN)Filariasis library which is an immune helminth phage display library[6] to isolate monoclonal antibodies against Strongyloides stercoralis (S. stercoralis) NIE recombinant protein (rNIE). This parasite causes strongyloidiasis, a potentially life-threatening disease with a complex diagnosis that impedes effective control and treatment of the disease. The difficulty of diagnosing this disease is mainly due to the sporadic output of larvae and serological cross-reactivity to other parasitic infections
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