Finally, the intrinsic properties of each protein, if available, were closely scrutinized. Therefore, proteins with hypothetical character were predominantly chosen, as information on them is confined. In addition, all types of membrane-associated proteins deserved a better look, as these type of proteins offer a more direct route and accessibility, which might be of utmost importance in a future rapid point-of care device detecting whole organisms. After epitope mapping, three of the six proteins under investigation revealed sites with potential linear epitopes. Still, the remaining proteins displayed no such sequences. This is, however, in accordance to the general prevalence of structural epitopes in comparison with linear epitopes in nature. In fact, approximately 90% of all epitopes are conformational rather than sequential. Despite these potential shortcomings of the used linear epitope mapping method, a number of intriguing linear epitopes have been identified. Notably, three proteins harbored sites with potential linear epitopes. Further careful examination, however, excluded KPN_00466 from future applications as the identified epitope sequence were nonspecific for K. pneumoniae, which might be due to the conserved character of the protein within the family Enterobacteriaceae. Still, KPN_00466 is a membrane protein and upcoming investigations might help to elucidate applications using this protein either for prevention of K. SANT-1 pneumoniae infections or detection thereof. This is well in line with the experimental results that indicate no binding by antibodies reactive to other bacteria to this sequence or any of its alterations. Moreover, alanine C646 scanning revealed a number of residues to be paramount for antibody binding. Consequently, replacing the glycine, alanine, alanine or either threonine leads to a significant loss of antibody binding observable by a dramatic reduction in signal intensity. On the contrary, removing either the first valine or leucine and inserting an alanine residue as a replacement results in a significant increase in signal intensity, potentially hinting at an improved antibody binding.