Structural characterisation, stability and antibody recognition of chimeric NHBA-GNA1030: An investigational vaccine component against Neisseria meningitidis

Highlights ► We describe the biophysical characteristics of the NHBA-GNA1030 vaccine antigen. ► The fusion protein has folded structure in the NHBA C-terminal domain and in GNA1030. ► Thermal stress causes little change in protein secondary structure. ► Exposure at 37 °C for up to 15 days results in...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Vaccine 2012-02, Vol.30 (7), p.1330-1342
Hauptverfasser:	Martino, Angela, Magagnoli, Claudia, De Conciliis, Giuseppe, D’Ascenzi, Sandro, Forster, Mark J, Allen, Lauren, Brookes, Charlotte, Taylor, Stephen, Bai, Xilian, Findlow, Jamie, Feavers, Ian M, Rodger, Alison, Bolgiano, Barbara
Format:	Artikel
Sprache:	eng
Schlagworte:	Adhesins, Bacterial - genetics Adhesins, Bacterial - immunology Adhesins, Bacterial - metabolism Allergy and Immunology Animals Antibodies, Bacterial - biosynthesis Antibodies, Bacterial - immunology antigens Antigens, Bacterial - genetics Antigens, Bacterial - immunology Antigens, Bacterial - metabolism chimerism chromatography Circular Dichroism electrophoresis Equilibrium unfolding fluorescence emission spectroscopy Fusion protein Heparin - immunology Heparin - metabolism Heparin binding antigen Hot Temperature immune response Immunoglobulin G - biosynthesis Immunoglobulin G - immunology Meningococcal Vaccines - genetics Meningococcal Vaccines - immunology Mice Mice, Inbred C57BL Models, Molecular Neisseria meningitidis Neisseria meningitidis, Serogroup B - immunology Protein Folding Protein Stability Protein Structure, Secondary Proteolysis Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - immunology serotypes Spectrometry, Fluorescence Spectrometry, Mass, Electrospray Ionization tryptophan vaccines
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	Highlights ► We describe the biophysical characteristics of the NHBA-GNA1030 vaccine antigen. ► The fusion protein has folded structure in the NHBA C-terminal domain and in GNA1030. ► Thermal stress causes little change in protein secondary structure. ► Exposure at 37 °C for up to 15 days results in protein degradation and aggregation. ► Maintenance of the intact, non-fragmented state preserves functional immunogenicity.
ISSN:	0264-410X 1873-2518
DOI:	10.1016/j.vaccine.2011.12.066