Abstract: This invention relates to immunogenic compositions including influenza B virus sequences, and methods of using such compositions.

Abstract: A chimeric polypeptide is disclosed that comprises: i) a first portion that self-assembles into an organized, repetitive, supramolecular structure that contains at least about 9 subunits, covalently linked to ii) a second polypeptide portion that comprises a peptide having a length of about 15 to about 80 amino acid residues. The second portion peptide self-assembles to form parallel multimers. A contemplated chimeric polypeptide forms a particle that is more stable than is a particle formed from a first polypeptide that is otherwise identical in sequence, but lacks the covalently linked self-binding peptide sequence of the second polypeptide portion.

Abstract: A chimeric, carboxy-terminal truncated hepatitis B virus nucleocapsid (HBc) protein is disclosed that contains an immunogen for inducing the production of antibodies to the influenza M2 protein. An immunogenic influenza sequence in two to four copies is preferably expressed at or near the N-terminus or in the HBc immunogenic loop sequence. The HBc chimer preferably contains an influenza-specific T cell epitope and is preferably engineered for both enhanced stability of self-assembled particles and enhanced yield of those chimeric particles. Methods of making and using the chimers are also disclosed.

Abstract: A chimeric, carboxy-terminal truncated hepatitis B virus nucleocapsid (core) protein (HBc) that is engineered for both enhanced stability of self-assembled particles and the substantial absence of nucleic acid binding by those particles is disclosed. The chimeric protein molecule can include one or more immunogenic epitopes peptide-bonded to one or more of the N-terminus, the immunogenic loop or the C-terminus of HBc. The enhanced stability of self-assembled particles is obtained by the presence of at least one heterologous cysteine residue near one or both of the amino-terminus and carboxy-terminus of the chimer molecule and the absence of the cysteine residues present in the native sequence at HBc positions 48 and 107.

Abstract: A chimeric, carboxy-terminal truncated hepatitis B virus nucleocapsid (HBc) protein is disclosed that contains an immunogen for inducing the production of antibodies to the influenza M2 protein. An immunogenic influenza sequence in two to four copies is preferably expressed at or near the N-terminus or in the HBc immunogenic loop sequence. The HBc chimer preferably contains an influenza-specific T cell epitope and is preferably engineered for both enhanced stability of self-assembled particles and enhanced yield of those chimeric particles. Methods of making and using the chimers are also disclosed.

Abstract: A chimeric, carboxy-terminal truncated hepatitis B virus nucleocapsid protein (HBc) is disclosed that contains an immunogen for inducing the production of antibodies to malarial proteins. An immunogenic malarial epitope is expressed between residues 78 and 79 of the HBc immunogenic loop sequence. The chimer preferably contains a malaria-specific T cell epitope and is preferably engineered for both enhanced stability of self-assembled particles and enhanced yield of those chimeric particles. Methods of making and using the chimers are also disclosed.