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Publikasjoner

NIBIOs ansatte publiserer flere hundre vitenskapelige artikler og forskningsrapporter hvert år. Her finner du referanser og lenker til publikasjoner og andre forsknings- og formidlingsaktiviteter. Samlingen oppdateres løpende med både nytt og historisk materiale. For mer informasjon om NIBIOs publikasjoner, besøk NIBIOs bibliotek.

2017

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Sammendrag

Infrared and 13C solid state nuclear magnetic resonance spectroscopies and benzene polycarboxylic acids (BPCA) analysis were used to characterize the structural changes occurring during slow pyrolysis of corncob and Miscanthus at different temperatures from 235 °C to 800 °C. In the case of corncob, a char sample obtained from flash carbonization was also investigated. Spectroscopic techniques gave detailed information on the transformations of the different biomass components, whereas BPCA analysis allowed the amount of aromatic structures present in the different chars and the degree of aromatic condensation to be determined. The results showed that above 500 °C both corncob and Miscanthus give polyaromatic solid residues with similar degree of aromatic condensation but with differences in the structure. On the other hand, at lower temperatures, char composition was observed to depend on the different cellulose/hemicellulose/lignin ratios in the feedstocks. Flash carbonization was found to mainly affect the degree of aromatic condensation.

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Sammendrag

Chronic Hepatitis B Virus (HBV) infection leads to severe liver pathogenesis associated with significant morbidity and mortality. As no curable medication is yet available, vaccination remains the most costeffective approach to limit HBV spreading and control the infection. Although safe and efficient, the standard vaccine based on production of the small (S) envelope protein in yeast fails to elicit an effective immune response in about 10% of vaccinated individuals, which are at risk of infection. One strategy to address this issue is the development of more immunogenic antigens. Here we describe a novel HBV antigen obtained by combining relevant immunogenic determinants of S and large (L) envelope proteins. Our approach was based on the insertion of residues 21-47 of the preS1 domain of the L protein (nomenclature according to genotype D), involved in virus attachment to hepatocytes, within the external antigenic loop of S. The resulting S/preS121-47 chimera was successfully produced in HEK293T and Nicotiana benthamiana plants, as a more economical recombinant protein production platform. Comparative biochemical, functional and electron microscopy analysis indicated assembly of the novel antigen into subviral particles in mammalian and plant cells. Importantly, these particles preserve both S- and preS1-specific epitopes and elicit significantly stronger humoral and cellular immune responses than the S protein, in both expression systems used. Our data promote this antigen as a promising vaccine candidate to overcome poor responsiveness to the conventional, S protein-based, HBV vaccine.