Impact of neutrophil‐activating protein conservation on diagnostic tests and vaccine design

BACKGROUNDThe neutrophil activating protein (NAP) is a highly immunogenic and virulence factor of Helicobacter pylori, presenting inflammatory and immunomodulatory activity. Consequently, NAP has been explored as a diagnostic and therapeutic target. However, when evaluating a target protein to design diagnostic methods or vaccines, it is critical to determine the protein conservation among the bacterial population, as well the impact of alterations of amino acid residues on the protein antigenic profile.RESULTSIn the present work, NAP conservation and theoretical antigenicity were determined among 51 sequences from H. pylori isolated from patients worldwide. A high NAP conservation (83%) was observed, where 17 amino acid residues, among the 144 residues of the protein, were polymorphic. Alterations at these polymorphic sites had a theoretically low impact on predicted antigenicity, where only 5 NAPs out of 51 NAPs presented a slightly different antigenic profile in relation to the consensus sequence. According to that, it was possible to recognize in western blotting 93% of NAP from different bacteria (n = 15) using polyclonal antibodies developed against a specific NAP.CONCLUSIONSIt was predicted that when working with polyclonal antibodies or large NAP fragments for diagnostic and vaccine design, slight variation in protein sequence will have a minimal impact on NAP recognition. However, if a NAP monoclonal antibody or small NAP epitopes are considered, it is critical to select the most conserved and antigenic NAP regions, to maximize the coverage of NAP variants. © 2024 Society of Chemical Industry (SCI).