Evidence map›Paper›PMID 42540298›Full record

ArticleACS omega2026

A Virus-Like-Particle-Based Conjugate Vaccine Targeting the Microtubule Binding Region of Tau Protein.

Hunter McFall-Boegeman, Cameron Talbot, Mauro Montalbano, Nicha Puangmalai, Kuang-Wei Wang, Meena Kannan, Jiaming Shi, Katrina Linning-Duffy, Setare Nick, Lily Yan and 3 more

Abstract read
In one paragraph

Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Hunter McFall-BoegemanDepartment of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States.ORCID https://orcid.org/0000-0002-9870-4326
Cameron TalbotDepartment of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States.
Mauro MontalbanoMitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, Texas 77555, United States.ORCID https://orcid.org/0000-0002-0456-452X
Nicha PuangmalaiMitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, Texas 77555, United States.
Kuang-Wei WangDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.
Meena KannanDepartment of Psychology, Michigan State University, East Lansing, Michigan 48824, United States.
Jiaming ShiDepartment of Psychology, Michigan State University, East Lansing, Michigan 48824, United States.
Katrina Linning-DuffyDepartment of Psychology, Michigan State University, East Lansing, Michigan 48824, United States.
Setare NickDepartment of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States.
Lily YanDepartment of Psychology, Michigan State University, East Lansing, Michigan 48824, United States.
Min-Hao KuoDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.
Rakez KayedMitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, Texas 77555, United States.ORCID https://orcid.org/0000-0001-6216-8640
Xuefei HuangDepartment of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States.ORCID https://orcid.org/0000-0002-6468-5526

Funding

Generation of active immunity against cytotoxic oligomeric tau speciesR01CA225105 · NCI · MICHIGAN STATE UNIVERSITY · PI HUANG, XUEFEI · 2018 to 2023
$2.8M
NCI NIH HHS R01 CA225105
6 · The paper itself

Abstract

There is a pressing need to develop novel strategies to ameliorate symptoms and slow the progression of Alzheimer's disease. One of the hallmarks of Alzheimer's disease is the high levels of tau protein, which can form toxic oligomers and characteristic neurofibrillary tangles in the brain. Antitau antibodies can potentially bind tau protein and reduce tau pathology. In order to elicit a powerful antitau antibody response, virus-like-particle bacteriophage Qβ-based conjugate vaccines were developed targeting the microtubule binding region of tau protein. The Qβ-tau vaccines were able to produce a strong antitau antibody response in not only wild-type mice but also in human tau transgenic mice and a llama. The levels of antibody induced were superior to those generated by a corresponding keyhole limpet hemocyanin-based tau conjugate mimicking the one vaccine that successfully completed phase 1/2 human clinical trials. The Qβ-tau vaccine significantly improved the cognitive functions of the immunized mice and reduced the levels of inflammatory cytokines and tau in the brains, suggesting its translational potential.

Identifiers

PMID42540298
PMCPMC13425505

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.