Year-end Sale % OFF 
Abstract
BackgroundIt has been documented that, independently from the specificity of the native antibody (Ab) for a given antigen (Ag), complementarity determining regions (CDR)-related peptides may display differential antimicrobial, antiviral and antitumor activities.Methodology/Principal FindingsIn this study we demonstrate that a synthetic peptide with sequence identical to VHCDR3 of a mouse monoclonal Ab (mAb) specific for difucosyl human blood group A is easily taken up by macrophages with subsequent stimulation of: i) proinflammatory cytokine production; ii) PI3K-Akt pathway and iii) TLR-4 expression. Significantly, VHCDR3 exerts therapeutic effect against systemic candidiasis without possessing direct candidacidal properties.Conclusions/SignificanceThese results open a new scenario about the possibility that, beyond the half life of immunoglobulins, Ab fragments may effectively influence the antiinfective cellular immune response in a way reminiscent of regulatory peptides of innate immunity.
Highlights
Antibodies (Abs) are formed by heavy and light chains composed of constant and variable regions
We investigated the immunomodulatory effects of the complementarity determining regions (CDR) of a human IgM monoclonal Abs (mAbs) (HuA) specific for difucosyl human blood group A substance, previously evaluated for their candidacidal properties [22], as well as the candidacidal and immunomodulatory effects of the CDRs of a mouse IgM mAb (MoA) which bind to the same carbohydrate epitope [21]
It has been documented that isolated CDR sequences, especially CDR H3, called micro-Abs may show the same binding properties and biological functions displayed by the native Ab [35,36]
Summary
Antibodies (Abs) are formed by heavy and light chains composed of constant and variable regions. The latter include six complementarity determining regions (CDRs) which constitute the antigen (Ag) binding-site. The structural repertoires and the relationships between amino acid sequences and tertiary structures have been extensively studied to reveal the importance of the typical loops, which are canonical structures in the three CDR segments belonging to the light chain (Ll, L2, and L3) as well as the first two CDR segments of the heavy chain (Hl and H2) [1]. The third CDR of the heavy chain (H3) displays wide variety in its length and amino acid sequence, and no canonical structures have ever been established for it [1,2,3]. It has been documented that, independently from the specificity of the native antibody (Ab) for a given antigen (Ag), complementarity determining regions (CDR)-related peptides may display differential antimicrobial, antiviral and antitumor activities
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
