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: The severe acute respiratory syndrome virus (SARS) is a coronavirus that instigated regional epidemics in Canada and several Asian countries in 2003. The newly identified SARS coronavirus (SARS-CoV) can be transmitted among humans and cause severe or even fatal illnesses. As preventive vaccine development takes years to complete and adverse reactions have been reported to some veterinary coronaviral vaccines, anti-viral compounds must be relentlessly pursued. In this study, we analyzed the effect of aurintricarboxylic acid (ATA) on SARS-CoV replication in cell culture, and found that ATA could drastically inhibit SARS-CoV replication, with viral production being more than 1000 fold than that in the untreated control. ATA is also shown to be an effective anti-viral for several other viruses, including West Nile Virus and variola virus.

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: We conducted feline calicivirus (FCV) inhibition experiment with two anti-viral aminohydrolases, asparaginase and glutaminase. We found that in the presence of 8 units and 4 units/ml of asparaginase, about 90% of FCV replication was inhibited. In contrast, glutaminase showed no significant inhibition effect on the virus replication. We have also shown that asparaginase did not inhibit the replication of adenovirus suggesting that the inhibition was specific. Our results implicated that asparaginase could be used as a candidate for anti-FCV drug development.