Solutions for Influenza Vaccine Development
Influenza A and B viruses cause significant annual morbidity and mortality. Worldwide estimates suggest 3-5 million severe illnesses and 290,000-650,000 respiratory deaths, leading to substantial economic impact (WHO 2020, 2019). Vaccination remains the cornerstone for mitigating seasonal influenza and pandemic preparedness. While existing influenza vaccines reduce infection rates and complications, their effectiveness is suboptimal. US data (2004-2018) shows average vaccine effectiveness against medically attended illness ranging from 10% to 60% (CDC 2020). More potent vaccines are urgently needed to improve influenza prevention and control.
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Evolution of Influenza Vaccine Substrates
The 1930s marked the development of cultivating influenza viruses in embryonated eggs. This method dominant until the 1950s. The discovery of influenza virus growth in various cell lines (MDCK and Vero cells) in the late 1950s led to a gradual shift from embryonated eggs to cells-based vaccine production.
Evolution of influenza vaccine substrates from embryonated eggs to cells.
Reviews in Medical Virology
Solutions for Enhanced Influenza Vaccine Development
Antigens for WHO's
Recommended Influenza
Vaccine Strains
• Encompassing the WHO's Latest Recommended Influenza Strains
• Validated Natural HA Trimer
• Validated Natural NA Tetramer
Solutions for Vaccine
Antigen Quantification and
Quality Control
• HA & NA Specific Antibodies
• Antibody Pair & Method Development Services
Vaccine Potency
Assessment Tools
and Services
• Humoral Immunity Assessment Methods Development Service (ELISA)
• Cellular Immune Assessment Kit (ELISpot)
Influenza’s constant antigenic drift necessitates annual vaccine reformulation for optimal efficacy. the WHO updates the formulation of the vaccine annually to ensure the vaccine match the seasonal circulating viruses. To support Influenza vaccine research and development, ACROBiosystems has developed key reagents consistent with influenza vaccine components recommended by WHO.
Antigens Encompassing the WHO's Latest Recommended Influenza Strain
| Flu Season |
WHO's Recommended Influenza Vaccine Strains |
Subtypes | Hemagglutinin (HA) | Neuraminidase (NA) |
|---|---|---|---|---|
| Northern hemisphere in 2025-2026 | A/Wisconsin/67/2022 | H1N1 | HA1-V52H7 | NEE-V524m |
| A/Victoria/4897/2022 | H1N1 | HA1-V52H8 | NEE-V524c | |
| A/Croatia/10136RV/2023 | H3N2 | H32-V52H4 | NEE-V524x | |
| A/District of Columbia/27/2023 | H3N2 | H32-V52H5 | NEE-V524x | |
| B/Austria/1359417/2021 | B/Victoria | HAE-V52H3 | NEE-V5245 | |
| B/Phuket/3073/2013 | B/Yamagata | HAE-V52H4 | NEE-V5246 | |
| Southern hemisphere in 2025 | A/Wisconsin/67/2022 | H1N1 | HA1-V52H7 | NEE-V524m |
| A/Victoria/4897/2022 | H1N1 | HA1-V52H8 | NEE-V524c | |
| A/Croatia/10136RV/2023 | H3N2 | H32-V52H4 | NEE-V524x | |
| A/District of Columbia/27/2023 | H3N2 | H32-V52H5 | NEE-V524x | |
| B/Austria/1359417/2021 | B/Victoria | HAE-V52H3 | NEE-V5245 | |
| B/Phuket/3073/2013 | B/Yamagata | HAE-V52H4 | NEE-V5246 | |
| Northern hemisphere in 2024-2025 | A/Wisconsin/67/2022 | H1N1 | HA1-V52H7 | NEE-V524m |
| A/Victoria/4897/2022 | H1N1 | HA1-V52H8 | NEE-V524c | |
| A/Thailand/8/2022 | H3N2 | H32-V52H3 | NEE-V524w | |
| A/Massachusetts/18/2022 | H3N2 | H32-V52H3 | NEE-V524v | |
| B/Austria/1359417/2021 | B/Victoria | HAE-V52H3 | NEE-V5245 | |
| B/Phuket/3073/2013 | B/Yamagata | HAE-V52H4 | NEE-V5246 | |
| Others | A/Wisconsin/588/2019 | H1N1 | HA1-V52H3 | NEE-V524k |
| A/Victoria/2570/2019 | H1N1 | HA1-V52H6 | NEE-V524e | |
| A/Sydney/5/2021 | H1N1 | HA1-V52H4 | NEE-V5248 | |
| A/Georgia/12/2022 | H1N1 | HAE-V52H7 | NEE-V524p | |
| A/Sydney/1304/2022 | H3N2 | HA2-V52H9 | NE2-V5247 | |
| A/Darwin/6/2021 | H3N2 | HA2-V52H5 | NEE-V5247 | |
| A/Darwin/9/2021 | H3N2 | HA2-V52H6 / HA2-V82E6 | NE2-V5249 | |
| A/Bangkok/1/1979 | H3N2 | HA2-V52H3 | / | |
| A/Hong Kong/483/97 | H5N1 | HA1-V5229 | / | |
| A/Vietnam/1194/2004 | H5N1 | HA1-V52H9 | / | |
| A/Thailand/1(KAN-1)/2004 | H5N1 | / | HA1-V5245 | |
| A /Guangdong/18SF020 | H5N6 | HA6-V52H3 | NEE-V524h | |
| A/turkey/Germany-MV/R2472/2014 | H5N8 | HA8-V52H3 | NEE-V5249 | |
| A/Shanghai/2/2013 | H7N9 | HA9-V5253 / HA9-V52H3 | / | |
| A/guinea fowl/Hong Kong/WF10/99 | H9N2 | HA1-V52H5 / HA2-V52H7 | / | |
| B/Singapore/WUH4618/2021 | B/Victoria | HAE-V52H6 | NEE-V524u | |
| B/Singapore/INFTT-16-0610/2016 | B/Yamagata | HAE-V52H5 | NEE-V524r |
Natural HA Trimer Assay Data
The purity of Influenza A [Victoria/4897/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H8) is more than 90% and the molecular weight of this protein is around 220-265 kDa verified by SEC-MALS.
Immobilized Influenza A [Victoria/4897/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H8) at 1 μg/mL (100 μL/well) can bind Human Anti-HA (H1N1) antibody3E1 with a linear range of 1-31.25 ng/mL (QC tested).
Human Anti-HA (H1N1) antibody3E1 captured on Protein A Chip can bind Influenza A [Victoria/4897/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H8) with an affinity constant of 4.64 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).
Influenza B virus [Austria/1359417/2021 (B/Victoria lineage)] Hemagglutinin (HA) Protein, His Tag (Cat. No. HAE-V52H8) binding to RBCs (Rooster red blood cells) at a final concentration of 0.4688 μg/mL can lead to complete hemagglutination. The final concentration of the sample in the first well was 15 μg/mL.
Natural NA Tetramer Assay Data
The purity of Influenza A (A/Sydney/1304/2022) Neuraminidase (NA) Protein, His Tag (Cat. No. NE2-V5247) is more than 90% and the molecular weight of this protein is around 50-70 kDa verified by SEC-MALS.
Immobilized Influenza A (A/Sydney/1304/2022) Neuraminidase (NA) Protein, His Tag (Cat. No. NE2-V5247) at 1 μg/mL (100 μL/well) can bind Anti-NA(A/PAN) Antibody,Mouse IgG with a linear range of 4-63 ng/mL (QC tested).
The assurance of vaccine potency is important for the timely release and distribution of influenza vaccines. Antigen quantification and quality control are important steps in evaluating vaccine effectiveness. ACROBiosystems provides key reagents for Influenza vaccine antigen quantification and quality control.
Potency assessment plays a crucial role in the development of influenza vaccines. It serves as a critical tool to evaluate the effectiveness and consistency of vaccine formulations. By potency testing ensures that vaccines meet regulatory standards for safety and efficacy. ACROBiosystems provides key reagents & service for Influenza vaccine potency assessment.
Humoral lmmunity Assessment Kits &Methods Development Service (ELISA)
| Product Type | Cat. No. | Product Description |
|---|---|---|
|
Influenza Virus Antigen Quantification Assay Kit |
RAS-A189 | Influenza A (H1N1) Viruses Hemagglutinin (HA) Specific ELISA Kit |
| RAS-A187 | Influenza A (H3N2) Viruses Hemagglutinin (HA) Specific ELISA Kit | |
| RAS-A210 | Influenza A/Darwin/9/2021 (H3N2) Virus Hemagglutinin (HA) Specific ELISA Kit | |
| RAS-A206 | Influenza B/Victoria Lineage Viruses Hemagglutinin (HA) Specific ELISA Kit | |
| RAS-A207 | Influenza B Viruses Hemagglutinin (HA) Specific ELISA Kit | |
| RAS-A191 | Influenza A [A/Bangkok/1/1979 (H3N2)] Hemagglutinin (HA) Specific ELISA Kit | |
| RAS-A193 | Influenza A [A/guinea fowl/Hong Kong/WF10/99(H9N2)] Hemagglutinin (HA) Specific ELISA Kit |
Customize your ELISA kit or method development service today！
FAQ
The available flu antibodies do not meet my specificity requirements. Is it possible to customize antibodies?
Yes, we offer customized antibody services. Our library includes over 100 antibodies, allowing us to efficiently identify and match products that align with your specific needs.
Are the HA and NA proteins provided by your company in their native structure?
The HA protein is provided in its trimeric structure, while the NA protein is in a tetrameric structure. This mimics the native structure of viral surface proteins and ensures reliability for your research.
The flu HA antigen protein HA1-V52H3, HAE-V52H3, and HA2-V52H5 all include trimeric components.
The mentioned products all feature trimeric components at the C-terminus, while the antibody binding epitopes are at the N-terminus, ensuring no interference with binding. ELISA validation shows good binding activity, with specific data available on the product webpage.
Resources
- Background
- Evolution of Influenza Vaccine Substrates
- Solutions for Enhanced Influenza Vaccine Development
- FAQ
- Resources