Abstract
Evidence from previous works disclosed the antimicrobial, antiviral, anti-tumour and/or immunomodulatory activity exerted, through different mechanisms of action, by peptides expressed in the complementarity-determining regions or even in the constant region of antibodies, independently from their specificity and isotype. Presently, we report the selection, from available databases, of peptide sequences encoded by immunoglobulin genes for the evaluation of their potential biological activities. Synthetic peptides representing the translated products of J lambda and J heavy genes proved to act in vitro against pathogenic fungi, entering yeast cells and causing their death, and exerted a therapeutic effect in a Galleria mellonella model of infection by Candida albicans. No haemolytic, cytotoxic and genotoxic effects were observed on mammalian cells. These findings raise the hypothesis that antibodies could be the evolutionary result of the adaptive combination of gene products ancestrally devoted to innate antimicrobial immunity.
Highlights
It is well known that the entire repertoire of human immunoglobulins (Igs) comprises such a vast number of different molecules to virtually recognise and bind to, through the antibody (Ab) variable region, any non-self structure, and even self-epitopes, as is the case of auto-Abs
We have shown that synthetic peptides with sequences identical to Ig fragments related to complementarity-determining regions (CDRs) and to constant domains can exert in vitro, ex vivo and/or in vivo antimicrobial, antiviral, immunomodulatory and/or anti-tumour activities, regardless of the specificity and isotype of the belonging Ab4–8
Synthetic peptides with the sequence of selected J lambda and J heavy gene products proved to display a fungicidal activity in vitro and a therapeutic activity in Galleria mellonella larvae against systemic candidiasis
Summary
It is well known that the entire repertoire of human immunoglobulins (Igs) comprises such a vast number of different molecules to virtually recognise and bind to, through the antibody (Ab) variable region, any non-self structure, and even self-epitopes, as is the case of auto-Abs. A naturally occurring IgM fragment proved to exert antifungal and antiviral activity, and showed a therapeutic effect against an experimental Candida albicans infection[9] These findings led to the speculation that the products of Ig genes could be endowed with innate anti-infective activity. Synthetic peptides with the sequence of selected J lambda and J heavy gene products proved to display a fungicidal activity in vitro and a therapeutic activity in Galleria mellonella larvae against systemic candidiasis These results support the hypothesis that genes encoding peptides ancestrally devoted to innate immunity may have been combined in the course of evolution to give rise to antibody molecules, characterised by highly specific activity, as effectors of adaptive immunity
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