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TitleStructural dynamics and immunogenicity of the recombinant and outer membrane vesicle-embedded Meningococcal antigen NadA.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateMar 11, 2026
AuthorsValeria Calvaresi / Lucia Dello Iacono / Sara Borghi / Enrico Luzzi / Alessia Biolchi / Ilaria Ferlenghi / Ilaria Peschiera / Fabiola Giusti / Lucia E Fontana / Zhong-Yuan Kan / Zaira Spinello / Marcello Merola / Isabel Delany / Kasper D Rand / Nathalie Norais /
PubMed AbstractStructural knowledge of antigens in their native state can drive the design of optimized vaccine antigens that mimic the native epitope exposure and conformation. Here, by hydrogen-deuterium exchange ...Structural knowledge of antigens in their native state can drive the design of optimized vaccine antigens that mimic the native epitope exposure and conformation. Here, by hydrogen-deuterium exchange mass spectrometry, we assessed the structural features of Neisseria Adhesin A (NadA), a meningococcal trimeric outer membrane protein, included as soluble recombinant antigen in the 4CMenB vaccine. We propose a structural annotation of the recombinant NadA and compare its structural dynamics with NadA in situ, as embedded in meningococcal outer membrane vesicles (OMVs). The observed conformational differences suggest that OMV-embedded NadA could be more susceptible to trimer opening and display a larger antigenic surface than the soluble antigen. Accordingly, mice immunized with OMV-embedded NadA elicited antibodies with superior bactericidal activity compared to the soluble antigen. Collectively, these data support the hypothesis that protein vaccine antigens presented in native-like environments can elicit a more potent immune response than recombinant forms.
External linksNat Commun / PubMed:41807399 / PubMed Central
MethodsEM (single particle)
Resolution14.2 Å
Structure data

EMDB-19474: N.meningitidis NadV3 surface expressed homotrimeric antigen structure
Method: EM (single particle) / Resolution: 14.2 Å

Source
  • Neisseria meningitidis (bacteria)
  • Neisseria meningitidis serogroup B (bacteria)

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