The HIV-1 virus employs a complex envelope protein to infiltrate human immune cells—primarily CD4+ T cells—making the envelope one of the most critical and vulnerable targets for neutralizing antibodies. Within this envelope, the V3 glycan site has consistently captured scientific attention because of its essential role in virus entry. Yet, previous attempts to exploit this site therapeutically have been hampered by the virus’s remarkable ability to mutate the glycan structures that antibodies typically recognize, enabling it to evade neutralization in many cases.

The antibody 007 breaks new ground by adopting a fundamentally different binding strategy. Unlike classical V3-targeting antibodies that rely on the presence of the N332 glycan—a sugar moiety on gp120, one subunit of the envelope trimer—007’s interaction with the epitope is glycan-independent. This means that the antibody can recognize and neutralize diverse HIV-1 variants regardless of their glycan modifications. Such versatility marks a critical leap forward because it significantly broadens the spectrum of virus strains against which the antibody is effective.

In rigorous in vitro neutralization assays, antibody 007 demonstrated robust activity against viral isolates that have historically shown resistance to classical V3 glycan antibodies. This resilience highlights the antibody’s potential as a powerful tool in both therapeutic and preventative contexts. The immune escape mechanisms that typically undermine monotherapies seem insufficient against 007, whose distinct binding not only neutralizes resistant strains but also complements existing antibody therapies to enhance overall efficacy.

To simulate human immune responses more accurately, the research team employed a humanized mouse model engrafted with human immune cells. Here, antibody 007 did not merely neutralize the virus; it synergistically amplified the effects of existing V3 antibodies. Combined therapy increased the evolutionary barrier for HIV, forcing the virus to undergo simultaneous, multiple mutations in order to escape. The implications of this are profound—raising the bar for viral resistance and thereby extending the clinical utility and durability of antibody-based treatments.

Structural and biophysical characterization of 007 revealed the molecular intricacies of its unique binding modality. Rather than locking onto a fixed glycan epitope prone to alteration, 007 targets an epitope configuration on gp120 that remains structurally conserved across a wide range of HIV-1 subtypes. This glycan-independent targeting minimizes the likelihood of escape mutations and supports the design of combination therapies that engage multiple vulnerable sites on the viral envelope simultaneously.

The discovery challenges prevailing assumptions within HIV vaccine research. By illustrating that the V3 glycan site can be exploited immunologically without reliance on the traditional glycan structures, 007 opens new avenues for vaccine design. Immunogens modeled to elicit antibodies with similar binding profiles could overcome the limitations of prior vaccine candidates that failed to induce breadth and potency sufficient for protective immunity.

Importantly, the translational potential of antibody 007 is already underway. The antibody has been exclusively licensed to Vir Biotechnology and is currently progressing through preclinical development with support from the Gates Foundation and the Cologne-based biotechnology startup Togontech. These partnerships underscore the real-world relevance of this research and its promise to yield next-generation HIV therapeutics and prophylactics, including passive immunization strategies.

This research embodies a significant advance in our understanding of HIV immunology and antibody engineering. By dissecting the nuanced mechanisms of HIV escape and unveiling a tool capable of bridging existing therapeutic gaps, the study sets a new benchmark for antibody discovery and development. Its findings are eagerly anticipated to catalyze further innovation in both treatment protocols and vaccine development pipelines.

Financial and institutional backing from the Gates Foundation, the German Research Foundation (DFG), the German Center for Infection Research (DZIF), and the European Research Council (ERC) have been instrumental in facilitating this milestone. These collaborations not only provided vital resources but also fostered a fertile environment for high-impact, interdisciplinary research.

Looking forward, the identification of 007 encourages the scientific community to reevaluate and expand the immunological targets considered ‘druggable’ within the HIV envelope. Its glycan-independent neutralization mechanism could inspire similar antibody discovery efforts against other challenging viral pathogens that employ glycan shields for immune evasion.

In summary, the antibody 007 represents a paradigm shift in HIV immunotherapy by effectively neutralizing a broad spectrum of viral variants through innovative epitope targeting. Its potential to complement and enhance existing V3-directed antibodies heralds a new era of multipronged antibody therapies, bringing us closer to the realization of durable HIV control and ultimately, prevention.

Subject of Research: People
Article Title: Identification of a potent V3 glycan site broadly neutralizing antibody targeting an N332gp120 glycan-independent epitope
News Publication Date: 3-Feb-2026
Web References: http://dx.doi.org/10.1038/s41590-025-02385-3
Image Credits: Klaus Schmidt
Keywords: HIV treatments, HIV infections, Vaccine research, HIV research, HIV prevention, Antibody therapy

IBV remains one of the most challenging pathogens confronting poultry farmers globally, including extensive losses in the United States. Current vaccination techniques predominantly involve live attenuated or killed virus formulations, which, despite widespread usage, carry inherent risks such as viral reactivation, mutation, or recombination — events that can culminate in vaccine-resistant or increasingly virulent strains. These traditional vaccines also suffer from limited shelf lives and the necessity of adjuvants—additives that enhance immune responses but complicate logistics and vaccine formulation stability.

The team led by Mazhar Khan, a distinguished professor in Pathobiology and Veterinary Science, in collaboration with Challa V. Kumar, an accomplished emeritus professor of Chemistry, has navigated these challenges by harnessing the transformative potential of mRNA vaccine technology. Prior to the global deployment of COVID-19 vaccines, the Kumar group had already conceptualized and synthesized a unique protein nanoparticle platform designed to overcome the core limitations of mRNA instability. This early innovation laid the groundwork for applying mRNA vaccination to IBV, where molecular precision and adaptive immune stimulation are paramount.

At the heart of this breakthrough lies a strategic chemical modification of bovine serum albumin, a naturally abundant, affordable, and biocompatible protein derived as a byproduct of beef production. By chemically attaching positively charged amine groups to the nanoparticle surface, researchers engineered a molecular vehicle capable of tightly binding the negatively charged mRNA strands. This robust electrostatic interaction not only shields the fragile mRNA from enzymatic degradation—particularly by nucleases prevalent in biological environments—but also facilitates targeted delivery to host cells, ensuring efficient expression of the virus’s spike protein antigen.

Extensive cellular assays and rigorous in vivo experimentation demonstrate that chickens immunized with this nanoparticle-mRNA complex mount an immune response dramatically superior to controls, with antibody titers against IBV amplified by a thousand-fold. Beyond humoral immunity, the vaccine markedly elevates cellular immune parameters, signaling a comprehensive activation of the avian immune system. These findings underscore the vaccine’s dual ability to create potent neutralizing antibodies while priming immune memory and effector mechanisms critical to long-term protection.

One of the critical practical hurdles addressed by this research is the inherent instability of mRNA, which rapidly degrades outside tightly controlled cold chain conditions. Such requirements impede vaccine distribution and application on farms, where infrastructure for ultra-low temperature storage is scarce or nonexistent. The protein nanoparticle platform resolves this issue by safeguarding the mRNA in situ, thus expanding the feasible handling and delivery conditions—a game changer in the realm of agricultural vaccine technology.

Conventional IBV vaccination demands labor-intensive individual injections for each chick, a process burdened by logistical inefficiency and animal welfare concerns. The UConn team is actively investigating alternative administration routes using aerosolized sprays that could coat the respiratory tract or skin of chicks en masse, drastically reducing labor and stress while maintaining vaccine efficacy. Such advancements promise to democratize vaccine delivery, enabling scalable interventions necessary for large poultry operations worldwide.

While IBV itself is not a human pathogen, the underlying technological innovation carries profound implications for human health. The nanoparticle platform’s modularity allows rapid incorporation of genetic sequences from emergent disease-causing organisms, paving the way for expedited mRNA vaccine development. This could redefine the pace and scope of vaccine responses not only during global pandemics but also for a wide array of infectious diseases that currently lack effective prophylaxis.

The collaborative synergy between biology, chemistry, and veterinary science at UConn exemplifies how interdisciplinary research can accelerate scientific breakthroughs with tangible societal impacts. The deliberate, methodical assembly of this nanoparticle-mRNA vaccine reflects years of incremental progress culminating in a practical solution poised to alleviate a persistent agricultural threat. Furthermore, the emphasis on affordability and scalability—rooted in the choice of bovine serum albumin and chemical modifications—reflects a deep understanding of end-user needs within the farming community.

As the researchers continue to optimize vaccine dosing, delivery mechanisms, and stability profiles, their work sets a new standard for pathogen-specific mRNA vaccines in veterinary medicine. Future studies will likely expand this platform’s application to other economically critical livestock diseases and potentially zoonotic infections, bridging a crucial gap between animal health and human disease preparedness.

Ultimately, this innovation highlights the immense promise of nanoparticle-mediated mRNA vaccine technologies beyond human health crises. By ensuring enhanced stability, targeted delivery, and potent immunogenicity, these protein-based nanoparticles embody a critical advancement capable of reshaping the landscape of infectious disease control in both agricultural and clinical domains.

Subject of Research: Animals

Article Title: Nanoparticle-Based mRNA Vaccine Induces Protective Neutralizing Antibodies Against Infectious Bronchitis Virus in In-Vivo Infection

News Publication Date: 26-May-2025

Web References:
10.3390/vaccines13060568

References: UConn research article in Vaccines, 2025

Keywords

Livestock, mRNA vaccine, nanoparticle, infectious bronchitis virus, poultry disease, veterinary science, vaccine stability, protein nanoparticle, immune response, bovine serum albumin

Traditional vaccines have largely depended on eliciting robust antibody responses, which primarily neutralize pathogens by binding to their surface antigens. However, these antibody titers wane over time, necessitating the administration of booster doses to maintain protective immunity. Moreover, rapidly mutating viruses such as influenza and SARS-CoV-2 frequently escape antibody surveillance through antigenic drift, undermining the durability and breadth of antibody-mediated protection. This well-documented challenge underscores the urgent need for next-generation vaccines that not only trigger antibody production but also induce durable cellular immunity capable of recognizing conserved viral or tumor epitopes. The WEHI research effort targets exactly this need by focusing on CD8+ T cells with stem cell-like properties, cells capable of rapid expansion and long-term survival, thus offering the prospect of vaccines with enduring efficacy.

Stem cell-like memory CD8+ T cells differ fundamentally from conventional effector or central memory T cells because of their stemness attributes—they can proliferate extensively upon antigen re-encounter, self-renew over long periods, and differentiate into potent cytotoxic effectors. These characteristics make them ideal candidates for sustaining long-lived protective immunity against diverse viral pathogens and tumor cells. Despite recognition of their importance, methods to selectively expand this T cell subset in vivo had remained elusive until now. Through the clever integration of mRNA vaccine technology and immunomodulatory interventions, the WEHI team successfully amplified this cell population in murine models, demonstrating a compelling link between their enhanced presence and improved vaccine outcomes.

Central to the study’s novel approach is the transient blockade of type I interferon (IFN) signaling during the vaccination window. Type I IFNs are critical cytokines in antiviral defense and immune regulation; however, their persistent activation can paradoxically impair the generation of effective memory CD8+ T cells by promoting terminal differentiation and exhaustion. By temporally inhibiting type I IFN responses, the researchers established a permissive milieu for stem cell-like memory T cell differentiation and expansion. This fine-tuned modulation preserved the delicate balance between immediate pathogen clearance and long-term immunological memory, effectively tilting the immune response towards durability and breadth. The implications of this finding extend beyond basic immunology, providing a robust mechanistic framework for rational vaccine design.

The innovative use of mRNA vaccine platforms in this context is particularly noteworthy. mRNA vaccines have revolutionized immunization strategies owing to their rapid development cycles, precise antigen encoding, and favorable safety profiles. Leveraging these characteristics, the WEHI investigators engineered mRNA vaccines that, combined with selective IFN pathway inhibitors, drove the robust generation of stem cell-like memory CD8+ T cells. This dual approach harnessed the intrinsic plasticity of mRNA vaccine technology while navigating immune signaling pathways to potentiate the quality and longevity of the T cell response. This synergy could herald a new paradigm wherein vaccines are customized not only for antigen specificity but also for tailored immune conditioning to maximize protective efficacy.

Beyond infectious disease applications, the study’s insights carry significant promise for cancer immunotherapy. CD8+ T cells are essential for recognizing and eliminating transformed cells through direct cytotoxic mechanisms. Enhancing the stemness and persistence of these T cells could overcome the current limitations posed by T cell exhaustion and tumor immune evasion. The researchers envision that their mRNA vaccine approach, optimized to amplify stem cell-like memory CD8+ populations, could become a powerful adjunct to existing cancer therapies, potentially transforming ‘cold’ tumors that are poorly infiltrated by immune cells into tumors amenable to immune-mediated eradication. This therapeutic potential aligns with the growing emphasis on personalized cancer vaccines aimed at stimulating robust and lasting cytotoxic T cell responses.

Associate Professor Joanna Groom, head of the Immunology division at WEHI and lead author of the study, emphasized the transformative potential of these findings. She highlighted how inducing these stem cell-like memory T cells addresses two formidable challenges in vaccinology: durability and breadth of protection. “We have long suspected that these cells underpin long-lasting immunity, but this study is the first to provide concrete proof of their benefit and, importantly, how to enhance them through vaccination,” Groom stated. Her remarks underscore the breakthrough nature of the work, which shifts the field’s focus from transient antibody titers towards sustained cellular immunity as the cornerstone of vaccine success.

The research team also pointed to the adaptability of their platform as a critical asset. Because mRNA vaccines can be rapidly redesigned to encode antigens from emerging viral variants or tumor neoantigens, the concurrent strategy of boosting stem cell-like memory CD8+ T cells creates a versatile and fast-reacting system poised to address future infectious threats and evolving cancers. This rapid responsiveness could streamline global vaccine deployment during pandemics and support personalized immunotherapy regimens customized to an individual’s tumor antigen profile, thus broadening the clinical applicability of their findings.

Crucially, the mouse model experiments demonstrated striking improvements in immune protection with the novel vaccine regimen. Mice vaccinated using the combined mRNA and transient IFN inhibition approach exhibited significantly higher levels of stem cell-like memory CD8+ T cells, which correlated strongly with superior control of infections and tumor challenge models. This compelling preclinical evidence lays a firm foundation for advancing the approach towards human clinical trials. If successfully translated, this strategy may reduce or obviate the need for frequent booster vaccinations, delivering sustained immunity intact for years or potentially decades following a single immunization course.

PhD student Benjamin Broomfield, first author on the paper, emphasized the therapeutic applicability of the system beyond infectious diseases. He remarked, “Our lab’s next frontier is to apply this vaccine platform to cancer treatment, where boosting these stem cell-like memory T cells could fundamentally improve patient outcomes by fueling durable anti-tumor immunity.” The optimism surrounding this endeavor reflects the broader movement in oncology to harness the immune system’s intrinsic capabilities for cancer eradication, potentially revolutionizing standard-of-care approaches and patient prognoses.

The study, titled Transient inhibition of type I interferon enhances CD8+ T cell stemness and vaccine protection, provides a mechanistic blueprint and practical roadmap for next-generation vaccines. It represents a powerful convergence of fundamental immunology, cutting-edge molecular technology, and translational biomedical research. As the world continues to confront the challenges posed by viral pandemics and intractable cancers, the WEHI team’s approach promises a future where vaccines offer not only immediate protection but lifelong immune resilience. The full details of this transformative research can be accessed through the Journal of Experimental Medicine.

Subject of Research: Cells
Article Title: Transient inhibition of type I interferon enhances CD8+ T cell stemness and vaccine protection
News Publication Date: 10-Mar-2025
Web References: DOI: 10.1084/jem.20241148
Image Credits: WEHI
Keywords: Vaccine research, T lymphocytes

Viruses, fundamentally simple yet cunning pathogens, rely heavily on their hosts’ cellular machinery to propagate. Because viral genomes are minimalistic, encoding only essential components, viruses must hijack host cellular processes to replicate and spread. One key evolutionary adaptation in herpesviruses involves the molecular mimicry of host kinases—enzymes that regulate the cell cycle and numerous signaling pathways through phosphorylation, a reversible chemical modification that switches protein activities on or off.

Cyclin-dependent kinases (CDKs) are central regulators of the eukaryotic cell cycle. They consist of two lobes (N- and C-lobes) with distinct structural and functional features. Phosphorylation at conserved serine, threonine, or tyrosine residues within the N-lobe modulates kinase activity, thus dictating cellular progression through specific cell cycle phases. Interestingly, certain herpesvirus protein kinases, termed conserved herpesvirus protein kinases (CHPKs), structurally mimic cellular CDKs, suggesting an evolutionary strategy to subvert host cell cycle controls.

Herpes simplex virus type 2 (HSV-2) is notorious for causing genital infections, meningitis, and severe neonatal diseases. It establishes lifelong latency in sensory neurons with intermittent reactivation episodes. Understanding the molecular underpinnings of HSV-2’s latency and reactivation cycles is pivotal for devising enduring antiviral interventions. The Japanese team, led by Professor Yasushi Kawaguchi and Assistant Professor Naoto Koyanagi, embarked on elucidating how HSV-2’s UL13 kinase—a CHPK—emulates CDK functionality and regulation via phosphorylation.

Employing cutting-edge molecular virology techniques, the researchers demonstrated that UL13 kinase undergoes phosphorylation at a conserved tyrosine residue (Tyr-162) within its N-lobe motif. This post-translational modification negatively regulates UL13’s catalytic activity. Experimental infections with wild-type HSV-2, UL13-deleted mutants, and a phosphorylation-deficient UL13-Y162F mutant revealed that phosphorylated UL13 is prevalent during later stages of viral replication, emphasizing a temporal regulatory role.

Notably, phosphomimetic mutations of this tyrosine residue attenuated kinase activity by diminishing phosphorylation of UL13 substrates. This fine-tuning effect was conserved across other herpesvirus subfamilies, underscoring a shared evolutionary mechanism of CDK mimicry and regulation. Functional assays showed that regulated phosphorylation modulates viral replication and pathogenicity during the lytic phase, particularly influencing viral virulence in murine brain infection models.

Intriguingly, while phosphorylation of UL13’s tyrosine residue suppressed acute viral replication, it was indispensable for viral reactivation from latency in guinea pigs. This duality suggests that UL13-mediated CDK mimicry orchestrates the delicate balance herpesviruses maintain between active lytic infection and latent persistence, optimizing viral survival and transmission over the host’s lifetime.

Phosphorylation-mediated regulation of viral kinases reflects a sophisticated layer of viral control, separate from but analogous to host cellular systems. This viral CDK mimicry does not merely copy enzymatic function but also incorporates intricate feedback loops via post-translational modifications, allowing herpesviruses to adapt dynamically to the intracellular environment and immune pressures.

The conservation of this motif and regulatory mechanism among diverse herpesviruses points to an ancient and successful evolutionary strategy. Moreover, the detection of similar conserved tyrosine phosphorylation motifs in viral kinases encoded by poxviruses suggests that this form of regulatory mimicry may extend beyond herpesviruses, revealing a broader paradigm in viral-host molecular interactions.

Professor Kawaguchi highlights the significance of these findings, emphasizing that uncovering the regulatory complexity of CHPK kinases not only advances the fundamental understanding of herpesvirus biology but also opens avenues for targeted antiviral drug design aimed at disrupting kinase regulation. Such approaches could interfere with viral replication dynamics without harming host kinase functions, offering precision therapeutic options.

Beyond immediate translational impacts, this work underscores the utility of viruses as biological probes. By decoding viral strategies such as CDK mimicry, researchers glean unique insights into cellular regulatory networks that are otherwise challenging to study. This reciprocal illumination enriches both virology and cell biology, fostering novel research trajectories and integrative biomedical innovations.

As herpesviruses continue to pose global health challenges through recurrent infections and associated diseases, deepening our comprehension of their molecular arsenal remains paramount. The delicate interplay of phosphorylation and kinase mimicry delineated in this study exemplifies the evolutionary ingenuity of viruses and represents a critical step toward disrupting their lifecycle through next-generation therapeutics.

Subject of Research: Cells

Article Title: Regulatory Mimicry of Cyclin-Dependent Kinases by a Conserved Herpesvirus Protein Kinase

News Publication Date: 16-Apr-2025

Web References:
https://www.pnas.org/doi/10.1073/pnas.2500264122

References:
Koyanagi, N., Hengphasatporn, K., Kato, A., Nobe, M., Takeshima, K., Maruzuru, Y., Maenaka, K., Shigeta, Y., & Kawaguchi, Y. (2025). Regulatory Mimicry of Cyclin-Dependent Kinases by a Conserved Herpesvirus Protein Kinase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2500264122

Image Credits:
Prof. Yasushi Kawaguchi from The University of Tokyo, Japan

Keywords:
Viruses, Herpesviruses, Enzymes, Kinases, Molecular Biology, Immunology, Cellular Processes, Phosphorylation, Viral Infections

The research led by Chi-Huey Wong, a distinguished chemistry professor at Scripps, posits that sugar molecules on the spike protein of coronaviruses serve as a protective shield. By removing these non-essential glycans through enzymatic processes, the vaccine enables the immune system to recognize and respond more effectively to the virus. Animal studies conducted during this research, particularly involving hamsters and mice, indicated that this approach produced a higher concentration of diverse antibodies, offering better protection than conventional vaccines that target individual strains.

Wong emphasized the unprecedented need for frequent updates to vaccines in response to mutations in the SARS-CoV-2 virus, underscoring the advantage of a universal vaccine. Targeting conserved, low-mutation regions of the virus allows this low-sugar vaccine to effectively prepare the immune system to respond not only to current variants but also to future coronavirus strains. The implications of this research extend beyond COVID-19, potentially covering other variants and related viruses, including those responsible for the flu and even the common cold.

Presenting his findings at the ACS Spring 2025 Digital Meeting, Wong details the mechanisms through which the vaccine operates. The breakthrough hinges on the identification of a stable region within the stalk of the viral spike protein, devoid of significant mutation. By eliminating the sugar molecules that typically obscure this region, Wong’s team was able to elicit a strong immune response, improving the specificity and efficacy of the antibodies generated against viral vectors.

The significance of Wong’s findings also lies in their potential application beyond viral infections. The same methodology that enabled the development of the low-sugar vaccine is being explored in other fields, such as oncology. Wong’s team is investigating the use of sugar manipulation to target cancer cells, a promising avenue that could revolutionize treatment strategies in oncology. Their recent publications in the Journal of the American Chemical Society reflect this dual focus on vaccines and cancer therapies, further underlining the versatility and potential impact of their research.

Conducted with the backing of Academia Sinica, the study contributes to a growing body of evidence suggesting that glycosylation plays a pivotal role in the interaction between pathogens and their hosts. By modulating the glycan structures present on viruses, researchers are uncovering new pathways to enhance vaccine efficacy. The low-sugar vaccine not only presents a solution to tackling rapidly mutating viruses but also introduces a paradigm shift in vaccine design, where carbohydrate structures are actively manipulated to achieve desired immune responses.

As the world continues to grapple with infectious diseases, this research opens up exciting possibilities for universal vaccination strategies. Wong’s universal vaccine may one day pave the way for a single-shot approach to immunization against an array of coronaviruses, greatly simplifying public health initiatives and improving global health outcomes. The promise of such vaccines lies not only in their effectiveness but also in their ability to ease the logistical burdens associated with mass vaccination campaigns, particularly in low-resource settings.

The research community eagerly anticipates the outcomes of an ongoing Phase I clinical trial, spearheaded by Rock Biotherapeutics, aimed to evaluate the safety and efficacy of this revolutionary vaccine in human subjects. Wong’s detailed insights during the ACS meeting will provide critical information on the future of this vaccine, aiding in the transition from laboratory findings to real-world solutions against viral infections.

With viral mutations consistently reshaping the landscape of infectious disease, the development of a low-sugar vaccine reflects a proactive approach in vaccine research. It embodies the spirit of scientific innovation, utilizing advanced biotechnology to refine the human immune response and fortify collective defenses against emerging health threats. The implications of this research are profound, as it represents a potential turning point in vaccination strategy that could usher in a new era of public health preparedness.

Ongoing dialogues within the scientific community regarding the utility of low-sugar vaccines may prompt additional research avenues, further enhancing our understanding of viral immunology and paving the way for next-generation therapeutics. As the findings from Wong’s studies continue to unfold, the scientific community remains hopeful and engaged, recognizing that the adaptation of vaccine strategies is essential in the ever-evolving battle against infectious diseases.

Importantly, the collaboration among researchers, healthcare professionals, and pharmaceutical entities will be crucial in moving this promising research from the bench to the bedside. This initiative not only encourages innovative applications of vaccine technology but also fosters a unified approach to combatting infectious diseases globally, building resilience through science and teamwork.

Subject of Research: Development of low-sugar universal vaccines targeting coronaviruses.
Article Title: Development of low-sugar universal vaccines and glycoengineered antibodies with improved Fc-mediated killing.
News Publication Date: March 25, 2025.
Web References: ACS Spring 2025 program.
References: Glycan targets on cancer cells; Enzymes linked to the synthesis of glycans on cancer cells.
Image Credits: Lorenzo Casalino.

Keywords

Vaccine development, COVID-19 vaccines, glycosylation, immunology, low-sugar vaccine, coronavirus, universal vaccine, animal studies, antibody diversity, public health.