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inactivated trivalent influenza vaccine (eTIV_f / Evagrip / Fluvirin)

✓ Approved

Novartis AG · 疫苗 · 疫苗

什么是 inactivated trivalent influenza vaccine？

inactivated trivalent influenza vaccine 是一种疫苗，由Novartis AG研发。该药已获批，用于治疗相关适应症，给药途径：Injectable (Others)、Intradermal Injection、Intramuscular (IM) Injection、Subcutaneous Injection。

药物档案

商品名eTIV_f, Evagrip, Fluvirin
公司Novartis AG
药物类别疫苗, 大分子
给药途径Injectable (Others), Intradermal Injection, Intramuscular (IM) Injection, Subcutaneous Injection
状态Approved
来源： ClinicalTrials.gov, Novartis AG

相关研究文献

PubMedVaccines2026-07-27

Evaluation of Immunogenicity and Cross-Protective Efficacy of a CpG-Adjuvanted Trivalent Inactivated Influenza Vaccine in Ferrets.

Qiu Yanping Y, Zhang Yan Y, He Shuangshuang S, Wang Yutian Y et al.

Background/Objectives: Pandemic influenza remains a persistent global threat, and while vaccination is the primary preventive measure, conventional vaccines often induce narrow, strain-specific immunity. This study evaluated the immunogenicity, protective efficacy, and cross-protective potential of a CpG-adjuvanted trivalent inactivated influenza vaccine (CpG-TIV) administered intramuscularly at high and low doses in ferrets. Methods: Groups of influenza-seronegative ferrets received two intramuscular injections, 3 weeks apart, of high- or low-dose CpG-TIV or a commercial non-adjuvanted trivalent vaccine. Three weeks after the second immunization (Day 42), serum was obtained, and the ferrets were subsequently challenged intranasally with homologous H1N1 and influenza B viruses, as well as a heterologous drifted H3N2 strain. Clinical signs, body weight, nasal viral load, and lung histopathology were monitored following the viral challenge. Results: CpG-TIV induced significantly higher dose-dependent HI and IgG antibodies than the commercial unadjuvanted vaccine. High-dose CpG-TIV markedly reduced weight loss, clinical symptoms, nasal viral load (by up to 99%), and lung pathological damage. Notably, high-dose CpG-TIV provided significant cross-protection against heterologous H3N2, whereas the commercial vaccine showed no protective effect. At Day 42, HI GMTs in the high-dose group reached 500, 254, and 594 against H1N1, H3N2, and B strains, respectively, with a maximal 2.58 log10 reduction in H1N1 viral load. Conclusions: High-dose CpG-TIV demonstrates strong immunogenicity and robust dose-dependent homologous and heterologous cross-protection in ferrets. The combination of a CpG adjuvant and high-dose antigen broadens protection against drifted influenza viruses, overcoming the narrow coverage of conventional vaccines. These data support further clinical development of this broad-spectrum influenza vaccine candidate.

PMID 42506652
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PubMedVaccines2026-07-27

Site-Specific Glycosylation Profiling of Protein Subunit and Inactivated Virus Vaccines.

Goecker Zachary C ZC, Burke Meghan C MC, Liu Yi Y, Mirokhin Yuri A YA et al.

Background/Objectives: Glycosylation can affect vaccine antigen structure and function, making site-specific glycan characterization relevant to antigen quality and comparability. However, quantitative approaches for comparing glycan microheterogeneity remain limited. This study evaluated the utility of the glycopeptide abundance distribution spectra framework for measuring similarity among site-specific glycosylation profiles in vaccines and antigen reference reagents across manufacturing conditions. Methods: Intact N-linked glycopeptides were characterized by nanoflow liquid chromatography-tandem mass spectrometry with stepped-energy fragmentation. Products included monovalent and quadrivalent influenza antigens produced in embryonated eggs, Madin-Darby canine kidney cells, or Spodoptera frugiperda cells, together with a SARS-CoV-2 spike vaccine produced in Spodoptera frugiperda cells and a Chinese hamster ovary cell-produced varicella-zoster virus glycoprotein E vaccine. Site-specific glycan distributions were represented as distribution spectra and compared using NIST MS Search software. Dot-product scores ranging from 0 to 999 quantified similarity. Results: Across measured glycosylation sites, distributions clustered into six recurrent classes. Similarity was high for replicate analyses, conserved influenza components across annual formulations, and matched components from different suppliers within the same production platform (similarity scores = 978, 961, and 960, respectively). Similarity was lower between sites within the same protein, between influenza strains, and between production sources (similarity scores = 554, 540, and 209, respectively). Among production-source comparisons, egg- and Madin-Darby canine kidney-derived profiles were most similar, and the overall ordering of glycosylation similarity was consistent with broad phylogenetic relatedness among production hosts. Conclusions: Distribution spectra-based similarity scoring of vaccine glycoproteins provides a quantitative, reusable approach for documenting site-specific glycosylation microheterogeneity. Using this method, we can conclude that production source is the dominant contributor to variation, whereas replicates, annual formulations, and suppliers within the same production platform are highly consistent.

PMID 42506681
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PubMedVaccines2026-07-27

Arming Inactivated Enveloped Virus Vaccines with the GGTA1 Gene: A Potent Method for Amplification of Viral Vaccines Effectiveness and Protection Against Variants.

Galili Uri U

This review describes a novel method for increasing the effectiveness of inactivated enveloped whole-virus vaccines by targeting them for extensive uptake by antigen-presenting cells (APCs). Several inactivated whole-virus vaccines with dense glycan shields display suboptimal effectiveness because the multiple carbohydrate chains (glycans) on the virus mask immunogenic peptides and surround the virus with a negative electrostatic charge that decreases uptake by APCs. It is postulated that engineering such vaccinating viruses to present the carbohydrate antigen "α-gal epitope" on the glycan shields will immunocomplex them with the anti-Gal antibody; thus, it will target them for robust uptake by APCs. Anti-Gal is an abundant natural antibody in humans, constituting ~1% of human circulating immunoglobulins. The ligand of anti-Gal is the α-gal epitope, which is naturally synthesized in non-primate mammals and New World monkeys by the glycosylation enzyme α1,3galactosyltransferase. This enzyme is encoded by the GGTA1-gene. Viral vaccines presenting multiple α-gal epitopes on their glycan shield bind anti-Gal and activate the complement system to produce complement chemotactic cleavage peptides C5a and C3a that induce extensive recruitment of APCs to vaccine injection sites. The virion-bound anti-Gal further targets the viral vaccine for robust uptake by APCs, following binding of its Fc "tail" to Fcγ-receptors on APCs. The efficacy of this method was studied in anti-Gal-producing mice with α-gal presenting inactivated influenza virus vaccine and with gp120 of HIV presenting this epitope. These studies indicated that virus vaccines engineered to present α-gal epitopes increase anti-virus antibody production and virus-specific T-cell activation by 15- to 100-fold in comparison to the same vaccines lacking α-gal epitopes. It is suggested that α-gal presenting inactivated SARS-CoV-2 virus vaccines can induce a similar protective long-term immune memory against S- M-, E-, and N-viral proteins. Furthermore, immune-escaping variants of the mutated S-protein may be destroyed by antibodies to M and E proteins, and cells infected with such variants may be killed by cytotoxic T cells specific to peptides of the N-protein. Such an anti-M-, E-, and N-protein immune protection may prevent expansion of these variants and thus may avoid the need for immunization with COVID-19 vaccines every 6 months or following the appearance of new variants. A similar potent immunization may be achieved with an inactivated Ebolavirus vaccine engineered to present α-gal epitopes on the glycan shield. The resulting immune response to the various Ebolavirus proteins also may contribute to cross-reactive protection against other Ebolavirus species containing proteins with evolutionarily conserved structures. An effective method for the preparation of a whole-virus vaccine presenting α-gal epitopes is by arming it with the GGTA1-gene inserted into the viral genome. Such virions will present multiple α-gal epitopes on their glycan shield, which will amplify their immunogenicity instead of reducing it in the wild-type virus.

PMID 42506608
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PubMedZhonghua yu fang yi xue za zhi [Chinese journal of preventive medicine]2026-07-27

[Research progress in combination vaccines containing sabin strain inactivated poliovirus vaccine].

Fu Y X YX, Cai L K LK, Liang J L JL, Zhao T T et al.

Sabin strain inactivated poliovirus vaccine (sIPV), derived from attenuated Sabin poliovirus strains, has emerged as a promising alternative to both oral poliovirus vaccine (OPV) and conventional inactivated poliovirus vaccine (cIPV). It eliminates the risk of vaccine-associated paralytic poliomyelitis (VAPP) and the emergence of vaccine-derived polioviruses (VDPVs). In addition, sIPV demonstrates superior biosafety and vaccine safety during production and administration compared with cIPV. The integration of sIPV into combination vaccines with other routine immunization antigens can reduce the number of injections and streamline immunization schedules, making sIPV-containing combination vaccines a key focus of recent research. Japan launched the world's first sIPV-containing tetravalent vaccine in 2012, followed by the introduction of an sIPV-containing pentavalent vaccine in 2024. In China, a standalone sIPV was licensed in 2015, and multiple sIPV-containing combination vaccines are currently in clinical trials or preclinical development. The primary challenges for these vaccines include antigen compatibility within combination formulations and the scalability of sIPV production. Future strategies, such as the use of innovative adjuvants and intradermal administration, may enable antigen-sparing approaches. This review provides a comprehensive summary of the development and application of sIPV-containing combination vaccines, aiming to inform and guide ongoing vaccine research and development in China.

PMID 42503940
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PubMedVaccines2026-07-27

Influenza B Vaccines: Current Landscape and Novel Development Strategies.

Kotlyarov Roman Y RY, Ravin Nikolai V NV, Mardanova Eugenia S ES

Influenza B virus (IBV) represents a significant global health threat, contributing 20-30% of annual influenza cases and causing substantial morbidity and mortality across all age groups. Current seasonal vaccines demonstrate variable effectiveness, highlighting the urgent need for next-generation approaches that provide enhanced and sustained protection against both IBV lineages. Moreover, continuous antigenic drift of circulating viruses progressively reduces the match between vaccine-induced antibodies and contemporary strains, necessitating broad-spectrum protection strategies. This review discusses influenza B virus control strategies, encompassing both conventional approaches and emerging vaccine technologies. While antiviral therapy, epidemiological surveillance, diagnostics, and non-pharmaceutical public-health measures are integral components of influenza B control, the present review focuses specifically on vaccine-based strategies. By critically appraising the available evidence, this review evaluates the extent to which these strategies may improve the effectiveness of IBV vaccines and, in the longer term, inform the prospect of reducing the burden of-or potentially eliminating-influenza B virus, a goal that remains hypothetical and requires clinical validation.

PMID 42506610
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PubMedVaccines2026-07-27

Strain Matching of Seasonal Influenza Vaccines and Emergence of Neuraminidase Inhibitor Resistance in China from 2015 to 2025.

He Peiqing P, Luo Junhao J, Pu Siyu S, Cui Simin S et al.

Background: Influenza remains a major global public health threat, and vaccination is one of the most effective preventive measures. However, frequent antigenic drift and occasional antigenic shift, along with the lead time required for vaccine development and regional differences in the evolution of circulating strains, may lead to mismatches between WHO-recommended vaccine strains and circulating viruses. In addition, antiviral resistance further complicates precise influenza prevention and control. Objectives: This study aimed to evaluate the concordance of vaccine strains with circulating influenza viruses and the emergence of neuraminidase inhibitor (NAI) resistance in China. Methods: Data on antigenic characterization and antiviral susceptibility testing were extracted from weekly influenza surveillance reports published by the Chinese National Influenza Center from 2015 to 2025. Viral evolution, substitutions at key antigenic sites, and resistance-associated mutations were further examined based on sequences of circulating influenza viruses in China. Results: The overall vaccine match rates were 95.72% (95% CI: 94.02-97.43%) for A(H1N1)pdm09, 58.96% (95% CI: 54.93-62.96%) for A(H3N2), 64.45% (95% CI: 59.49-69.41%) for B/Victoria, and 95.19% (95% CI: 91.32-99.05%) for B/Yamagata in China during the 2015-2025 influenza seasons, with marked year-to-year fluctuations observed particularly for A(H3N2) and B/Victoria. The vaccine matching for cell-based A(H3N2) (70.41%, 95% CI: 65.04-75.77%) vaccine reference strains was significantly higher than that for egg-based A(H3N2) (48.09%, 95% CI: 42.63-53.55%) vaccine reference strains. Sequence analysis indicated that circulating A(H3N2) viruses showed the greatest genetic divergence from the matched egg-based vaccine strains (2.71%, 95% CI: 2.66-2.75%). Phenotypic NAI resistance was detected only in A(H1N1)pdm09 viruses, with resistance rates of 0.18% (95% CI: 0.07-0.45%) in 2023, 3.47% (95% CI: 2.63-4.57%) in 2024, and 3.01% (95% CI: 2.46-3.68%) in 2025. Neuraminidase (NA) sequence analysis showed that the key NAI resistance-associated substitution H274Y has been detected in A(H1N1)pdm09 viruses since 2015, at relatively high frequencies observed during 2015-2018. The mutation re-emerged in 2023 and presented increase trends thereafter, although no A(H1N1) pdm09 circulated during the COVID-19 pandemic. Conclusions: Antigenic concordance between vaccine strains and circulating A(H3N2) or B/Victoria viruses showed marked year-to-year fluctuations in China. Cell-based A(H3N2) vaccine reference strains showed higher antigenic concordance than egg-based strains, supporting further consideration of vaccine production platforms in A(H3N2)-predominant seasons. Phenotypic NAI resistance in circulating A(H1N1)pdm09 viruses was detected from 2023 onward in China, whereas resistance-associated NA substitutions had been detected earlier at the sequence level.

PMID 42506623
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