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Structural organization of NadADelta(351-405), a recombinant MenB vaccine component, by its physico-chemical characterization at drug substance level.

Abstract：

:The physico-chemical characterization of NadADelta(351-405), a recombinant protein discovered by reverse vaccinology, component of a candidate vaccine against Neisseria meningitidis serotype B is presented. Analytical methods like mass spectrometry, electrophoresis, optical spectroscopy and SEC-MALLS have been applied to unveil the structure of NadADelta(351-405), and to evaluate Product-Related Substances. Moreover, analysis of the protein after intentional denaturation has been applied in order to challenge the chosen methods and to determine their appropriateness and specificity. All the obtained results were inserted in a model allowing in-depth understanding of the antigen NadADelta(351-405): it is present in solution as a homo-trimer, retaining a high percentage of alpha-helix secondary structure, and able to reassemble from monomeric subunits after thermal denaturation; this structural organization is consistent with that foreseen for MenB NadA (Neisseria Adhesin A). The analytical data sets produced during process development for clinical phases I-III material confirm product quality and manufacturing consistency.

journal_name

Vaccine

journal_title

Vaccine

authors

Magagnoli C,Bardotti A,De Conciliis G,Galasso R,Tomei M,Campa C,Pennatini C,Cerchioni M,Fabbri B,Giannini S,Mattioli GL,Biolchi A,D'Ascenzi S,Helling F

doi

10.1016/j.vaccine.2009.01.099

subject

Has Abstract

pub_date

2009-03-26 00:00:00

pages

2156-70

issue

15

eissn

0264-410X

issn

1873-2518

pii

S0264-410X(09)00162-5

journal_volume

27

pub_type

杂志文章

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