High heterogeneity of cross-reactive immunoglobulins in multiple sclerosis presumes combining of B-cell epitopes for diagnostics: a case-control study.

Background: Multiple sclerosis (MS) is a neuroinflammatory disease triggered by a combination of genetic traits and external factors. Autoimmune nature of MS is proven by the identification of pathogenic T cells, but the role of autoantibody-producing B cells is less clear. A comprehensive understanding of the development of neuroinflammation and the identification of targeted autoantigens are crucial for timely diagnosis and appropriate treatment.

Characterization of Structural Properties and Antimicrobial Activity of the C3f Peptide of Complement System.

The C3f peptide is a by-product of regulation of the activated complement system with no firmly established function of its own. We have previously shown that C3f exhibits moderate antimicrobial activity against some Gram-positive bacteria . Presence of two histidine residues in the amino acid sequence of the peptide suggests enhancement of its antimicrobial activity at lower pH and in the presence of metal cations, particularly zinc cations.

Two-dimensional high-throughput on-cell screening of immunoglobulins against broad antigen repertoires.

Identifying high-affinity antibodies in human serum is challenging due to extremely low number of circulating B cells specific to the desired antigens. Delays caused by a lack of information on the immunogenic proteins of viral origin hamper the development of therapeutic antibodies. We propose an efficient approach allowing for enrichment of high-affinity antibodies against pathogen proteins with simultaneous epitope mapping, even in the absence of structural information about the pathogenic immunogens.