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influenza HA vaccine

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Denka Seiken · · Vaccine

What is influenza HA vaccine?

influenza HA vaccine is a vaccine developed by Denka Seiken. It is approved for therapeutic indications via injectable (others) or subcutaneous injection.

Drug Profile

CompanyDenka Seiken
Drug ClassVaccine, Large Molecules
Molecular Target,
RouteInjectable (Others), Subcutaneous Injection
StatusApproved
Sources: ClinicalTrials.gov, Denka Seiken

Mechanism of Action

Molecular Targets

influenza HA vaccine acts on 2 molecular targets:

(HA)
(HA)
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Related Research Articles

PubMedVirologica Sinica2026-07-17

Pygenic Acid A, a Small-Molecule PD-1/SHP-2 Inhibitor, Enhances Efficacy of Therapeutic Melanoma Vaccines and Prophylactic Influenza Vaccines.

Yan Yan Y, Li Yitong Y, Mei Wenyi W, Li Yixin Y et al.

Overcoming immunosuppressive tumor microenvironments remains a critical challenge in advanced vaccine development. Here, we evaluated Pygenic acid A (PA), an intracellular small-molecule inhibitor targeting the PD-1/SHP-2 axis, as a novel vaccine adjuvant. The adjuvant efficacy of PA was systematically assessed in two murine models: a therapeutic B16-F10 melanoma lung metastasis model and a prophylactic lethal H1N1 influenza virus challenge model. In the melanoma metastasis model, PA potentiated the anti-tumor effect of the mTRP2 vaccine, markedly inhibiting pulmonary metastatic lesions and prolonging the survival of tumor-bearing mice. Mechanistically, PA robustly boosted the intratumoral infiltration of functional T cells, thereby reversing local tumor immunosuppression. In the influenza vaccination model, consistent immunostimulatory effects were observed: the PA-adjuvanted hemagglutinin (HA) vaccine effectively elicited broad-spectrum cross-neutralizing antibody responses and provided complete protection against lethal heterologous influenza virus challenge. Further mechanistic investigations demonstrated that PA specifically promoted the differentiation of T follicular helper (Tfh) cells and the expansion of germinal center (GC) B cells in draining lymph nodes, while triggering a robust Th1-type cellular immune response dominated by IFN-γ secretion. Furthermore, in vivo safety assessments verified that PA intervention induced no obvious systemic inflammation, hematological abnormalities, or visceral organ injury, indicating a favorable safety profile. Collectively, these results demonstrate that PA serves as a potent and safe intracellular checkpoint-targeting adjuvant capable of potentiating both cellular immunity and cross-protective humoral immunity, holding great translational promise for the development of advanced cancer vaccines and broad-spectrum influenza vaccines.

PMID 42462877
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PubMedFrontiers in veterinary science2026-07-17

A trivalent inactivated PDCoV-PEDV-TGEV vaccine confers protective efficacy in piglets coinfected with porcine rotavirus.

Zha Yinhe Y, Yu Xiaoyu X, Duan Yu Y, Zhang Wentao W et al.

Porcine epidemic diarrhea virus (PEDV), porcine deltacoronavirus (PDCoV), and transmissible gastroenteritis virus (TGEV) are the primary enteric coronaviruses responsible for viral diarrhea in piglets. These pathogens frequently co-circulate with porcine rotavirus (PoRV) under field conditions, leading to increased disease severity and complicating prevention efforts. Although multivalent vaccines targeting these three coronaviruses have been developed, their protective efficacy in the presence of PoRV coinfection remains largely unknown. Based on our previously developed trivalent inactivated PDCoV-PEDV-TGEV vaccine, the present study evaluated its immunoprotective efficacy in piglets naturally infected with PoRV. The results showed that, despite the background of persistent PoRV infection, the trivalent vaccine induced detectable neutralizing antibodies against PEDV, PDCoV, and TGEV (titers≥1:64). Furthermore, vaccination significantly reduced fecal viral shedding after challenge, shortened the duration of diarrhea, and alleviated intestinal pathological damage. Immunofluorescence assays confirmed that antigen deposition of the target coronaviruses in the intestines of vaccinated piglets was markedly reduced. However, vaccinated piglets continued to shed PoRV, indicating that the vaccine did not confer sterilizing immunity but rather reduced clinical severity. This study provides the experimental evidence that the trivalent inactivated vaccine confers effective protection against the three major porcine enteric coronaviruses even under complex clinical conditions involving PoRV coinfection. These findings offer important insights for developing immunization strategies to control multi-pathogen infections in swine production.

PMID 42465716
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PubMedmedRxiv : the preprint server for health sciences2026-07-17

Post-vaccination expansion of extrafollicular Th10 and regulatory Tfr cells distinguishes strong from weak influenza vaccine responses in older adults.

Mahajan Avinash S AS, Ravichandran Sathyabaarathi S, Marches Radu R, Yazici Yilmaz Yucehan YY et al.

Despite the superior efficacy of high-dose influenza vaccines, over one-third of older adults fail to respond. Yet, the mechanisms underlying this impaired vaccine responsiveness remain poorly understood. Here, we performed longitudinal profiling of older adults (n=60) receiving high-dose influenza vaccination to identify immune programs associated with vaccine responsiveness. Strong responders exhibited a primed baseline immune state characterized by elevated plasma cytokines and chemokines, followed by enhanced IFN-γ responses and coordinated transcriptional and epigenetic activation of cDC2 cells at day 1. By day 7, CD4⁺ T-cell trajectories diverged: strong responders preferentially expanded influenza-specific activated cTfh1 ( CXCR5 + CXCR3 + ICOS + CD38 + ) and influenza-specific Th10 ( CXCR5⁻ CXCR3 + PD1 + IL10⁺ ) cells, whereas weak responders expanded regulatory cTfr ( CXCR5⁺ FOXP3⁺ ) cells. Th10 expansion correlated with plasmablast and antibody responses and was independently validated in a larger influenza vaccination cohort, including younger adults. Functionally, Th10 cells promoted memory B-cell differentiation into plasmablasts and production of influenza-specific IgGs. TCR analyses revealed minimal clonal overlap between Th10 and cTfh1 cells. Together, these findings identify divergent helper and regulatory CD4⁺ T cell programs associated with vaccine responsiveness and establish Th10 cells as a previously unrecognized component of vaccine-induced humoral immunity.

PMID 42465941
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PubMedMedicinal research reviews2026-07-17

Current Development of Small Molecules Against Influenza A Virus by Targeting Hemagglutinin.

Xu Dandan D, Gu Xinpeng X, Yu Qiao Q, Dou Xinyu X et al.

Influenza A virus (IAV) continues to be one of the most serious health burdens causing widespread illness and mortality. Limited efficacy and reduced susceptibility of available drugs and vaccines to the emergence of resistant strains have spurred the pursuit of alternative treatment strategies. Hemagglutinin (HA), essential for viral attachment and membrane fusion in the first step of the virus infection cycle, has emerged as an attractive target. Over the past few decades, HA has garnered considerable attention, and significant progress has been achieved in the discovery of HA modulators, even though no anti-IAV drugs targeting HA have been approved by the FDA. This article provides a comprehensive overview of the current landscape of HA inhibitors and degraders, mainly focusing on the systematic structure-activity relationship (SAR) exploration of both synthetic and natural product (NP)-derived small molecules endowed with abundant structural frameworks, together with a brief introduction of different binding modes based on cocrystal structures of IAV HAs and HA inhibitors. We anticipate that this review will serve as practical guidance for the development of urgently needed, more effective, and structurally innovative HA-targeting drugs capable of addressing the escalating challenge of drug resistance.

PMID 42464963
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PubMedBioconjugate chemistry2026-07-17

Synthesis of Glycooligomers with Defined Sialyllactose Valency and Spacing for Multivalent Binding to Influenza Hemagglutinin.

Kumon Yusuke Y, Nagao Masanori M, Matsumoto Hikaru H, Tsuji Sotaro S et al.

Influenza A virus is a medically important target. Hemagglutinin (HA), a trimeric glycoprotein on the viral surface, recognizes sialylated glycans through three receptor-binding sites. Glycoligands that interact with HA through multivalent binding can serve as viral inhibitors. To achieve efficient multivalent binding, precise control over glycoligand structures is essential. Here, we synthesized glycooligomers displaying sialyllactose units at defined intramolecular spacings and investigated how ligand structure affects binding to HA. Glycooligomers displaying one, two, or three sialyllactose units at regular intervals exhibited enhanced binding as carbohydrate valency increased. When the spacing between two sialyllactose units was varied, shorter spacing enhanced binding, likely because of a statistical rebinding effect. Interestingly, the presentation of an excessive number of sialyllactose units weakened the interaction with HA, presumably because of steric hindrance. These findings highlight the importance of precise carbohydrate arrangement in the design of effective multivalent ligands.

PMID 42463633
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PubMedbioRxiv : the preprint server for biology2026-07-17

The microprotein Dafcin resembles influenza HA fusion peptide and regulates the size of storage lysosomes in the germline.

Nyberg Kevin G KG, Easterlin Ryder R, Stringer Cooper W P CWP, Küçükengin Hamdi K HK et al.

Microproteins translated from short open reading frames are increasingly understood to play important roles in cell biology and development. Here, we describe a microprotein in Drosophila that is expressed in ovarian follicle cells which surround the developing oocyte. The Dafcin microprotein is predicted to form an amphipathic alpha-helix, a structure known to interact with lipid bilayers. Dafcin's structure most resembles the influenza HA fusion peptide, which induces negative curvature of endosomal membranes. Dafcin tagged with GFP localizes to the Golgi and is ultimately secreted from the follicle cells. Remarkably, this occurs without the microprotein having a secretory signal sequence. The protein is taken up into the oocyte by endocytosis, localizing to the inner face of storage lysosomes called yolk granules. Mutant analysis shows that Dafcin is required to limit the size of yolk granules. This may occur by inducing negative membrane curvature like HA peptide. In support, liposomes formed in vitro with both Dafcin and HA peptides are smaller in size.

PMID 42465374
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