Recombinant Protein of Immunogenic Metabolic Enzyme Epitopes of Trichomonas vaginalis are Common to Humans and Microorganisms

Abstract

Protein Immunogenic Metabolic Enzyme Epitopes vaginalis are Common to Abstract The number one, non-viral sexually transmitted infection (STI) worldwide is caused by the ancient protist . Recently, I reported on an ~40-kDa String-Of-Epitopes chimeric protein (AEG::SOE2) consisting of immunogenic epitopes unique to the vaginalis fructose-1,6bisphosphate aldolase (A), α -enolase (E), and glyceraldehyde-3-phosphate dehydrogenase (G). This report is on another construct of a 49.41-kDa AEG::SOE3 chimeric protein comprised of 8, 9 and 12 non-unique, immunogenic epitopes of A, E and G, respectively. These non-unique epitopes were detected by sera of women and men patients but not control, seronegative sera of women and men. The epitopes were found to have ≥50% to 100% sequence amino acid sequence identity with the human homolog and homologs of Candida albicans, Escherichia coli, Saccharomyces cerevisiae, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes as well as the homologs of the STI agents Chlamydia trachoma- tis, Neisseria gonorrhoeae and Treponema pallidum . The AEG::SOE3 protein was not detected by mouse anti AEG::SOE2 serum and by monoclonal antibodies (MAbs) to AEG::SOE2, showing the distinctness of these two chimeric proteins. AEG::SOE3 was detected by ELISA and immunoblot with sera of mice immunized with fixed T. vaginalis organisms, with sera of women and men patients with trichomonosis, and with MAbs to AEG::SOE3. The patient sera reactive to these immunogenic metabolic enzyme epitopes of AEG::SOE3 may be indicative of immune-crossreactive antibodies to human proteins during this STI. The role of these possible immune-crossreactive antibodies produced during this STI and those conceivably gener- ated by other STIs and microbial pathogens to heretofore unappreciated disease pathogenesis is discussed.