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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.<\/jats:p><\/jats:sec><jats:sec><jats:title>RESULTS<\/jats:title><jats:p>In the present work, NAP conservation and theoretical antigenicity were determined among 51 sequences from <jats:italic>H. pylori<\/jats:italic> 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 (<jats:italic>n<\/jats:italic>\u2009=\u200915) using polyclonal antibodies developed against a specific NAP.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONCLUSIONS<\/jats:title><jats:p>It 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. \u00a9 2024 Society of Chemical Industry (SCI).<\/jats:p><\/jats:sec>","DOI":"10.1002\/jctb.7755","type":"journal-article","created":{"date-parts":[[2024,9,17]],"date-time":"2024-09-17T14:39:57Z","timestamp":1726583997000},"page":"80-89","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Impact of neutrophil\u2010activating protein conservation on diagnostic tests and vaccine design"],"prefix":"10.1002","volume":"100","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6799-2740","authenticated-orcid":false,"given":"L\u00eddia MD","family":"Gon\u00e7alves","sequence":"first","affiliation":[{"name":"iMed.UL \u2013 Research Institute for Medicines and Pharmaceutical Sciences Faculdade de Farm\u00e1cia da Universidade de Lisboa  Lisbon Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7807-4726","authenticated-orcid":false,"given":"Ant\u00f3nio J","family":"Almeida","sequence":"additional","affiliation":[{"name":"iMed.UL \u2013 Research Institute for Medicines and Pharmaceutical Sciences Faculdade de Farm\u00e1cia da Universidade de Lisboa  Lisbon Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5264-9755","authenticated-orcid":false,"given":"Cec\u00edlia RC","family":"Calado","sequence":"additional","affiliation":[{"name":"ISEL \u2013 Instituto Superior de Engenharia de Lisboa Instituto Polit\u00e9cnico de Lisboa  Lisbon Portugal"},{"name":"iBB \u2013 Institute for Bioengineering and Biosciences, i4HB \u2013 Associate Laboratory Institute for Health and Bioeconomy, IST \u2013 Instituto Superior T\u00e9cnico Universidade de Lisboa  Lisbon 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