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influenza virus vaccine (FluShield)

✓ Approved

Pfizer, Inc. · Vaccine · Vaccine

What is influenza virus vaccine?

influenza virus vaccine is a vaccine developed by Pfizer, Inc.. It is approved for therapeutic indications via injectable (others) or intramuscular (im) injection.

Drug Profile

Brand NamesFluShield
CompanyPfizer, Inc.
Drug ClassVaccine, Large Molecules
RouteInjectable (Others), Intramuscular (IM) Injection
StatusApproved
Sources: ClinicalTrials.gov, Pfizer, Inc.

Related Research Articles

PubMedAdvances in virology2026-09-20

Comparative Sequence Analysis of the Envelope Gene of Kyasanur Forest Disease Virus Vaccine Strain With Currently Circulating Field Strains.

Kaje Keerthi K, Marinaik Chandranaik B CB, Gomes Amitha Reena AR, Rizwan Apsana A et al.

The present study was undertaken with the objective of performing comparative sequence analysis of the envelope (E) gene of Kyasanur forest disease virus (KFDV) vaccine strain P9605 with the circulating field strains. The study was taken up as the currently used KFDV vaccine strain, KFDV P9605, was isolated in the 1960s. For this study, we designed two sets of primers targeting the complete amplification of the E gene of KFDV. The sequencing was performed by the Sanger method, and the deduced sequence of the vaccine virus was deposited in GenBank with accession number PX067005. This sequence obtained for the vaccine virus was aligned and compared with sequences of GenBank-deposited circulating field strains. We also performed comparative sequence analysis of the Kyasanur forest disease (KFD) vaccine seed virus having passaged twice in mouse brain with the vaccine seed virus passaged six times in mouse brain to investigate whether multiple passages in mouse brain will lead to genetic mutation in the immunologically important E gene. The phylogenetic analysis revealed seven amino acid mutations in the field strains at positions A123T, S158N, D178E, D239N, A313S, M429I, and G479A when compared with the vaccine strain. We did not find any mutations at the critical fusogenic segment (residues 98-113) in the E gene of currently circulating field strains compared to the vaccine seed virus. The study found no genetic variations in the E gene of the KFD virus passed two times and passed six times in mouse brain. We performed SWISS-MODEL homology modeling, AlphaFold protein analysis, and Ramachandran plot analysis to study the E protein structures and stability. The observations made in this study suggest slow evolutionary drift and conserved structural stability of the envelope gene of KFDV ever since its emergence 7 decades ago; however, the functional implications of these amino acid substitutions need further studies on their roles in viral infectivity, transmission, and impact on immunity.

PMID 42763584
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PubMedEMBO reports2026-09-20

TRIM62 facilitates influenza A virus entry by regulating WASH-dependent endosomal trafficking.

Gupta Kajal K, Pal Sampurna S, Tyagi Arpit A, Bajaj Roohani R et al.

Endocytosis enables efficient cargo uptake while restricting uncontrolled cellular entry, yet how this balance is enforced during endocytic uptake remains poorly understood. Using influenza A virus (IAV) as a model cargo, we reveal a previously unrecognized role for the pentameric WASH complex (WASH) as a regulatory hub that integrates both permissive and inhibitory functions to control viral endocytosis. While the WASH subunits WASH1, CCDC53, SWIP, and Strumpellin collectively promote IAV entry, the FAM21 subunit acts antagonistically. Our data suggest that FAM21-mediated association of WASH with the retromer subunit VPS35 restrains the pro-endocytic activity of WASH, thereby limiting viral uptake. This inhibitory FAM21-VPS35 axis is counteracted by the E3 ubiquitin ligase TRIM62, which maintains WASH in a retromer-free, endocytically competent state that facilitates viral internalization. Beyond IAV, the WASH1 subunit and VPS35 also exhibit opposing roles during cholera toxin B uptake, suggesting a broader function in lipid raft-mediated endocytosis. Together, our findings establish WASH as a key determinant of IAV endocytosis, with TRIM62 modulating retromer-mediated restriction to facilitate productive viral entry.

PMID 42763336
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PubMedJournal of inflammation research2026-09-20

Dimethyl Sulfoxide Modulates T Cell-Mediated Immunity to Attenuate Influenza A Virus Infection.

Jeng Po-Hsuan PH, Tsai Meng-Wei MW, Huang Shing-Hwa SH, Huang Tien-Ru TR et al.

Influenza A virus (IAV) remains a major threat because vaccines provide limited cross-protection and antiviral resistance is rising. Dimethyl sulfoxide (DMSO) is immunomodulatory, but its effect on IAV has not been tested in vivo. We evaluated its efficacy and mechanism in a murine H1N1 model. Male C57BL/6 mice were intranasally challenged with an LD50 of A/Puerto Rico/8/1934 (H1N1) and given daily subcutaneous DMSO (0.22 g/kg/day) or phosphate-buffered saline (PBS) on days 1-7. Survival was monitored for 21 days; lung and bronchoalveolar lavage fluid (BALF) were collected on day 8. Lung histology (hematoxylin and eosin), BALF cytokines (sandwich ELISA), lung and splenic IFN-γ-producing CD4+ and CD8+ T cells (flow cytometry), and whole-lung RNA sequencing (differential expression, KEGG enrichment) were assessed. BALF viral burden was measured by neuraminidase activity assay and TCID50. In vitro, splenic CD8+ T cells exposed to 0%, 0.5%, or 1.0% DMSO were immunoblotted for lymphocyte-activation gene 3 (LAG3). DMSO significantly improved 21-day survival and attenuated alveolar inflammatory infiltration. Day-8 BALF viral titers were significantly lower with DMSO (mean 2.2×103 vs 4.3×104 TCID50/mL; p = 0.034), as was neuraminidase activity. BALF IFN-γ and TGF-β were elevated, whereas TNF-α, IL-6, and IL-1β were not. IFN-γ+ CD8+ T cells increased in the lung but not the spleen; CD4+ populations were unchanged. RNA sequencing showed enrichment of cytokine-cytokine receptor interaction and PI3K/Akt signaling and upregulation of T-box factors, PPAR-γ, and Nek kinases. In vitro, DMSO accelerated LAG3 induction in CD8+ T cells within 12-48 h. DMSO is associated with attenuated IAV severity, a lower day-8 airway viral burden, and a localized expansion of IFN-γ-producing CD8+ T cells, without a concomitant rise in the pro-inflammatory cytokines TNF-α, IL-6, or IL-1β. These associations are correlative and support further investigation of DMSO as a host-directed adjunct for influenza.

PMID 42763701
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PubMedVeterinary medicine international2026-09-20

Pattern of Cytopathic Effects Produced by Recent Bangladeshi Field Isolates of PPR Virus in Vero Cells and Preparation of Purified Viral Antigen.

Siddiqui M S I MSI, Begum Jahan Ara JA, Islam M R MR, Chowdhury E H EH

This study was conducted to explore the pattern of appearance of cytopathic effect (CPE) produced by a Bangladeshi strain of Peste des petits ruminant's virus (PPRV) in Vero cells during serial passaging, to estimate the virus titer and concentration of PPR viral RNA at different passage levels, and to find out a suitable passage level for viral antigen purification. Five isolates of PPR virus from local outbreaks were isolated, confirmed with conventional RT-PCR, and then used as viral inoculant in Vero cells and lamb kidney cell culture (LKC). Morphology of CPE's and pattern of development of CPE were studied and recorded at different passage levels and days postinfection (dpi). Tissue culture fluid (TCF) was used to prepare purified viral antigen by ultracentrifugation and for quantitation by spectrophotometry. Viral titers were determined following an endpoint dilution assay. The study revealed that the CPE was not perceptible in all isolates until 11 dpi for the first six passages. The virus was not detected in TCF of both infected and control flasks by RT-PCR up to the 6th passage. The first CPE appeared on 5 dpi at the 7th passage level for all isolates. The CPE was characterized by initial cell rounding, followed by the formation of small syncytia, progression to total cell infection, and eventual complete detachment of the cell monolayer. Maximum titer (3.5 Log10TCID50) and RNA concentration (260 ng/µL) were found at the 30th passage level by one isolate (Isolate-F). It is concluded that initiation of CPE production in Vero cells by the Bangladeshi field strain of PPR virus occurs at the 7th passage level. Virus titer and concentration of PPR viral RNA increased with the advancement of passaging, and these are highly related to each other. TCF at higher passage levels, such as the 60th passage, is most suitable for purification of PPR viral antigen.

PMID 42763559
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PubMedVeterinary research2026-09-20

Mapping of three novel linear B-cell epitopes on the VP7 protein of epizootic hemorrhagic disease virus with monoclonal antibodies.

Hu Xinbing X, Zhong Yunru Y, He Yingjuan Y, Zhang Mingxin M et al.

Epizootic hemorrhagic disease virus (EHDV) is an important Orbivirus transmitted by culicoides midges. EHDV poses a significant threat to ruminant production worldwide. The VP7 protein is a highly conserved, group-specific antigen of EHDV, which serves as a key target for serological diagnosis. In this study, the recombinant VP7 (r-VP7) protein of EHDV-1 was expressed in an Escherichia coli expression system and used to immunize BALB/c mice. Four hybridoma cell lines secreting monoclonal antibodies (mAbs) against VP7 were successfully generated by the hybridoma technique, and named 5D1, 6A7, 7B11, and 7C4. Indirect ELISA, western blot analysis, and immunofluorescence assays demonstrated that all four mAbs specifically recognized both the r-VP7 protein and the native VP7 protein in EHDV-1-infected BHK-21 cells, with favorable reactivity and specificity. The VP7 protein was progressively truncated and expressed as a series of GST fusion proteins, and the linear B-cell epitopes recognized by these mAbs were precisely identified by western blotting. The results showed that 5D1 and 7B11 recognized the epitope 83DYIQNLATIGVLATPEI99, 7C4 recognized 121PDRQPFGYFL130, and 6A7 recognized 229APVNVNNPGQ238. Sequence alignment and cross-reactivity assays revealed that the three epitopes were highly conserved among EHDV serotypes and showed no cross-reactivity with the VP7 proteins of African horse sickness virus (AHSV) or bluetongue virus (BTV). Three-dimensional structural analysis indicated that all three epitopes were exposed on the surface of the VP7 trimer and were located in distinct structural domains. In summary, this study successfully generated four specific mAbs against the EHDV VP7 protein and identified three novel linear B-cell epitopes, providing a foundation for the development of specific EHDV serological diagnostic methods and epitope-based vaccines.

PMID 42763396
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PubMedViruses2026-09-20

Correction: Villalba et al. Development and Validation of Three Triplex Real-Time RT-PCR Assays for Typing African Horse Sickness Virus: Utility for Disease Control and Other Laboratory Applications. Viruses 2024, 16, 470.

Villalba Rubén R, Tena-Tomás Cristina C, Ruano María José MJ, Valero-Lorenzo Marta M et al.

In the original publication [...].

PMID 42763783
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