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

authorProfile.emailbiblioteca@isel.pt
datacite.subject.fosEngenharia e Tecnologia::Engenharia Química
dc.contributor.authorDiogo Gonçalves, Lídia Maria
dc.contributor.authorAlmeida, António J.
dc.contributor.authorCalado, Cecília
dc.date.accessioned2025-04-02T11:52:25Z
dc.date.available2025-04-02T11:52:25Z
dc.date.issued2025-01
dc.description.abstractBACKGROUND: The 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. RESULTS: In 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. CONCLUSIONS: 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.por
dc.description.sponsorshipIPL/IDI&CA/R-DICIP_ISEL - Instituto Politécnico de Lisboa (IPL)
dc.identifier.citationGonçalves, L. M. D.; Almeida, A. J.; & Calado, C. R. C. (2025). Impact of neutrophil-activating proteinconservation on diagnostic tests andvaccine design. Journal of Chemical Technology & Biotechnology, 100(1): 80-89. https://doi.org/10.1002/jctb.7755
dc.identifier.doihttps://doi.org/10.1002/jctb.7755
dc.identifier.eissn1097-4660
dc.identifier.issn0268-2575
dc.identifier.urihttp://hdl.handle.net/10400.21/21737
dc.language.isoeng
dc.peerreviewedyes
dc.publisherWiley
dc.relationDSAIPA/DS/0117/2020 - Fundação para a Ciência e a Tecnologia (FCT)
dc.relationPTDC/ BIO/69242/2006 - Fundação para a Ciência e a Tecnologia (FCT)
dc.relationUID/DTP/04138/2013 - Fundação para a Ciência e a Tecnologia (FCT)
dc.relation.hasversionhttps://scijournals.onlinelibrary.wiley.com/doi/epdf/10.1002/jctb.7755
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectHelicobacter pylori
dc.subjectNAP
dc.subjectImmunogenic
dc.subjectGenetic variability
dc.subjectNeutrophil-activating protein
dc.subjectImmunovariability
dc.titleImpact of neutrophil-activating protein conservation on diagnostic tests and vaccine designeng
dc.typeresearch article
dspace.entity.typePublication
oaire.citation.endPage89
oaire.citation.issue1
oaire.citation.startPage80
oaire.citation.titleJournal of Chemical Technology and Biotechnology
oaire.citation.volume100
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
person.familyNameDiogo Gonçalves
person.familyNameCalado
person.givenNameLídia Maria
person.givenNameCecília
person.identifier130332
person.identifier.ciencia-id7211-22BA-86AD
person.identifier.ciencia-id9418-E320-3177
person.identifier.orcid0000-0002-6799-2740
person.identifier.orcid0000-0002-5264-9755
person.identifier.ridE-2102-2014
person.identifier.scopus-author-id6603163260
relation.isAuthorOfPublication3f8540f5-bc6b-4e10-94c5-7d0325b7fa3f
relation.isAuthorOfPublicatione8577257-c64c-4481-9b2b-940fedb360cc
relation.isAuthorOfPublication.latestForDiscovery3f8540f5-bc6b-4e10-94c5-7d0325b7fa3f

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