Despite many years of research, serodiagnosis of Lyme disease still faces many obstacles. Difficulties arise mainly due to the low degree of amino acid sequence conservation of the most immunogenic antigens among B. burgdorferi s.l. genospecies, as well as differences in protein production depending on the environment in which the spirochete is located. Mapping B-cell epitopes located on antigens allows for a better understanding...

Currently, the diagnosis of Lyme disease is based mostly on two-tiered serologic testing. In the new generation of immunoenzymatic assays, antigens comprise whole-cell lysates of members of the Borrelia burgdorferi sensu lato (s.l.) species complex, with the addition of selected recombinant proteins. Due to the high diversity of members of the B. burgdorferi s.l. genospecies and the low degree of conservation among the amino acid...

The diverse antigenic structure of Borrelia burgdorferi sensu lato (s.l.) and the low degree of protein sequence conservation between genospecies causes many limitations in serodiagnosis of Lyme disease (LD). Using expression systems based on Escherichia coli, five monovalent B. burgdorferi s.l. recombinant proteins were produced. i.e., BB0108, BB0126, BB0298, BB0323, BB0689 (each in three variants derived from Borrelia afzelii,...

Lyme disease is a tick-borne zoonosis caused by Gramnegative bacteria belonging to the Borrelia burgdorferi sensu lato (s.l.) group. In this study, IgM- and IgG-specific linear epitopes of two B. burgdorferi sensu stricto (s.s.) antigens BmpA and BBK32 were mapped using a polypeptide array. Subsequently, two chimeric proteins BmpABBK32-M and BmpA-BBK32-G were designed to validate the construction of chimeras using the identified...