Abstract: A synthetic hemagglutinin (sHA) which represents the highest degree of conservation in the HA sequences of all Influenza B viruses (IVB) based on comprehensive bioinformatics analyses was cloned into an adenoviral vector. The recombinant adenovirus carrying the sHA gene was then delivered intransallyintranasally into DAB/2 mice. The animals were challenged with 5xLD50 influenza B viruses. We have found that the synthetic HA vaccines afford 100% protection against lethal challenge whereas 50% mice died in the control group. Furthermore, no virus was found in the lung of the vaccinated group while significant lung viruses were found in all mice of the controlled group. Consistent with the survival data and virus titre, severe pneumonia was found in all mice of the control group while no pathologic observation was made in animals receiving the vaccines.

Abstract: A synthetic hemagglutinin (sHA) which represents the highest degree of conservation in the HA sequences of all Influenza B viruses (IVB) based on comprehensive bioinformatics analyses was cloned into an adenoviral vector. The recombinant adenovirus carrying the sHA gene was then delivered intransallyintranasally into DAB/2 mice. The animals were challenged with 5xLD50 influenza B viruses. We have found that the synthetic HA vaccines afford 100% protection against lethal challenge whereas 50% mice died in the control group. Furthermore, no virus was found in the lung of the vaccinated group while significant lung viruses were found in all mice of the controlled group. Consistent with the survival data and virus titre, severe pneumonia was found in all mice of the control group while no pathologic observation was made in animals receiving the vaccines.

Abstract: Two universally conserved sequences from influenza type A neuraminidases were identified by large scale sequence analysis then chemically modified and conjugated to carrier proteins to generate mono-specific and monoclonal antibodies. The two antibodies, one targeting the N-terminus of the type A neuraminidase and the other sequence close to enzymatic active site, were capable of binding to all 9 subtypes of neuraminidase while demonstrating remarkable specificity against the viral neuraminidase sequences since no cross-reactivity against allantoic proteins was observed. Quantitative analyses of NA using slot blot suggest that the antibodies can be used for NA antigen quantitation in vaccines. These represent the first time the antibody-based immunoassay can be used for NA quantitative determination.

Abstract: Two universally conserved sequences from influenza type A neuraminidases were identified by large scale sequence analysis then chemically modified and conjugated to carrier proteins to generate mono-specific and monoclonal antibodies. The two antibodies, one targeting the N-terminus of the type A neuraminidase and the other sequence close to enzymatic active site, were capable of binding to all 9 subtypes of neuraminidase while demonstrating remarkable specificity against the viral neuraminidase sequences since no cross-reactivity against allantoic proteins was observed. Quantitative analyses of NA using slot blot suggest that the antibodies can be used for NA antigen quantitation in vaccines. These represent the first time the antibody-based immunoassay can be used for NA quantitative determination.

Abstract: Two universally conserved sequences from influenza type A neuraminidases were identified by large scale sequence analysis then chemically modified and conjugated to carrier proteins to generate mono-specific and monoclonal antibodies. The two antibodies, one targeting the N-terminus of the type A neuraminidase and the other sequence close to enzymatic active site, were capable of binding to all 9 subtypes of neuraminidase while demonstrating remarkable specificity against the viral neuraminidase sequences since no cross-reactivity against allantoic proteins was observed. Quantitative analyses of NA using slot blot suggest that the antibodies can be used for NA antigen quantitation in vaccines. These represent the first time the antibody-based immunoassay can be used for NA quantitative determination.

Abstract: Two universally conserved sequences from influenza type A neuraminidases were identified by large scale sequence analysis then chemically modified and conjugated to carrier proteins to generate mono-specific and monoclonal antibodies. The two antibodies, one targeting the N-terminus of the type A neuraminidase and the other sequence close to enzymatic active site, were capable of binding to all 9 subtypes of neuraminidase while demonstrating remarkable specificity against the viral neuraminidase sequences since no cross-reactivity against allantoic proteins was observed. Quantitative analyses of NA using slot blot suggest that the antibodies can be used for NA antigen quantitation in vaccines. These represent the first time the antibody-based immunoassay can be used for NA quantitative determination.

Abstract: Two universally conserved sequences from influenza type A neuraminidases were identified by large scale sequence analysis then chemically modified and conjugated to carrier proteins to generate mono-specific and monoclonal antibodies. The two antibodies, one targeting the N-terminus of the type A neuraminidase and the other sequence close to enzymatic active site, were capable of binding to all 9 subtypes of neuraminidase while demonstrating remarkable specificity against the viral neuraminidase sequences since no cross-reactivity against allantoic proteins was observed. Quantitative analyses of NA using slot blot suggest that the antibodies can be used for NA antigen quantitation in vaccines. These represent the first time the antibody-based immunoassay can be used for NA quantitative determination.

Abstract: The present invention discloses isolated peptides encoding an antigen or fragments thereof from the N-terminus of hemagglutinin protein of influenza, methods for isolating such antigens and specific uses thereof. The peptide can be used as a vaccine to generate an antibody response that neutralizes influenza infectivity against a variety of influenza strains.

Abstract: Antibodies that specifically bind to a peptide having an amino acid sequence as found at the N-terminus of the HA2 fusion peptide of the influenza A virus may be raised by inoculating a mammal with a conjugate of the peptide. In one embodiment, the conjugate comprises the peptide linked to a spacer (e.g. 6-aminocaproic acid) and a carrier protein (e.g. KLH). The antibodies may be used as a universal reagent for detecting HA proteins of influenza viruses. The antibodies are useful as versatile reagents for laboratory research and vaccine potency determination, especially in the event of pandemic influenza outbreaks.

Abstract: Two universally conserved sequences from influenza type A neuraminidases were identified by large scale sequence analysis then chemically modified and conjugated to carrier proteins to generate mono-specific and monoclonal antibodies. The two antibodies, one targeting the N-terminus of the type A neuraminidase and the other sequence close to enzymatic active site, were capable of binding to all 9 subtypes of neuraminidase while demonstrating remarkable specificity against the viral neuraminidase sequences since no cross-reactivity against allantoic proteins was observed. Quantitative analyses of NA using slot blot suggest that the antibodies can be used for NA antigen quantitation in vaccines. These represent the first time the antibody-based immunoassay can be used for NA quantitative determination.

Abstract: The present invention discloses isolated peptides encoding an antigen or fragments thereof from the N-terminus of hemagglutinin protein of influenza, methods for isolating such antigens and specific uses thereof. The peptide can be used as a vaccine to generate an antibody response that neutralizes influenza infectivtty against a variety of influenza strains.

Abstract: Antibodies that specifically bind to a peptide having an amino acid sequence as found at the N-terminus of the HA2 fusion peptide of the influenza A virus may be raised by inoculating a mammal with a conjugate of the peptide. In one embodiment, the conjugate comprises the peptide linked to a spacer (e.g. 6-aminocaproic acid) and a carrier protein (e.g. KLH). The antibodies may be used as a universal reagent for detecting HA proteins of influenza viruses. The antibodies are useful as versatile reagents for laboratory research and vaccine potency determination, especially in the event of pandemic influenza outbreaks.