First, we have been able to identify a previously unknown antigenic site TLIKELKRLGI of cj0669 from C. jejuni and were able to determine the important residue involved in antibody binding as well as modelling the epitope’s accessibility within the full-length protein. For C. jejuni the generation of monoclonal antibodies against cj0669 is mandatory to further Amikacin hydrate investigate the affinity and kinetics of the observed binding event by BIAcore. This might grant further insight whether or not this sequence is a suitable candidate for specific detection in a biosensor or if cj0669 is a suitable vaccine candidate. Mutagenesis of cj0669 might help to illuminate the function of this protein and its Catharanthine sulfate potential role if any in pathogenicity. Once this is determined, a monoclonal antibody might be used to cocrystallize the antigen for X-ray crystallography to assign a measured structure to the predicted model. On top of that, antibody validation by ELISA with a wide array of C. jejuni isolates is needed to evaluate the applicability of the derived antibody for future clinical point-of-care devices. Additionally, next-generation sequencing of transcriptomes of a broad spectrum of C. jejuni strains ought to be beneficial in analyzing the presence and expression of the protein. This might provide further insight into the suitability of the protein for clinical applications and vaccine development. Consequently, it could help to identify potential sequence homologies or discrepancies, which as of now are limited to already published datasets. Thus, nextgeneration sequencing might be an attractive procedure to complement the approach presented herein. Secondly, we have established and applied a quick and easy method for the screening of cDNA expression libraries in order to rapidly detect novel immunodominant proteins of bacteria, see Figure 8 for a summary. The information needed prior to analysis is minute, yet using fully sequenced strains is advantageous as it speeds up the identification of genes and proteins. Still, even unsequenced strains such as clinical isolates can easily be analyzed and should not pose any hindrance, as homologous proteins ought to be identified via BLAST. The more important prerequisite for the screening is the availability of polyclonal antibodies or patient sera. In the context of a diagnostic tool to be used in hospitals, patient sera are beneficial, as they resemble the desired immune response better, thus narrowing down the results to the clinically most relevant proteins. Finally, suitable references are useful, yet in most cases, some immunodominant antigens have already been described. Regardless, even without a suitable known antigen, this method could identify novel immunoreactive proteins and their linear epitopes with some minor adjustments to the overall calculations. In conclusion, we have successfully shown the application of this method while gaining insight into some novel immunodominant proteins of an important gut pathogen, C. jejuni. The current research emphasizes the need for future investigations in two distinct areas. First, more insight into the newly identified proteins of C. jejuni might foster the understanding of this enigmatic pathogen and help to illuminate its pathogenicity while providing suitable means for rapid detection and combating its spreading. Second, transferring this method to other bacterial pathogens will help to discover other immunodominant proteins, potentially leading to a broad spectrum of clinical applications and serological assays. Additionally, it might be preferable to simplify the identification of conformational epitopes as this could greatly enhance the retrieval rate of suitable antigenic sites.