Evidence map›Paper›PMID 39060263›Full record

ArticleScientific reports2024

A novel monoclonal antibody generated by immunization with granular tau oligomers binds to tau aggregates at 423-430 amino acid sequence.

Yoshiyuki Soeda, Emi Hayashi, Naoko Nakatani, Shinsuke Ishigaki, Yuta Takaichi, Taro Tachibana, Yuichi Riku, James K Chambers, Riki Koike, Moniruzzaman Mohammad and 1 more

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

11 authors.

Yoshiyuki SoedaLaboratory for Alzheimer's Disease, Department of Life Science, Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo, 171-8588, Japan. soeday7188@gmail.com.
Emi HayashiCell Engineering Corporation, 5-12-14 Nishinakajima, Yodogawa-ku, Osaka, 532-0011, Japan.
Naoko NakataniCell Engineering Corporation, 5-12-14 Nishinakajima, Yodogawa-ku, Osaka, 532-0011, Japan.
Shinsuke IshigakiDepartment of Diagnostics and Therapeutics for Brain Disease, Molecular Neuroscience Research Center, Shiga University of Medical Science, Seta Tsukinowa-cho, Otsu, Shiga, 520-2192, Japan.
Yuta TakaichiLaboratory of Veterinary Pathology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Taro TachibanaCell Engineering Corporation, 5-12-14 Nishinakajima, Yodogawa-ku, Osaka, 532-0011, Japan.
Yuichi RikuInstitute for Medical Science of Aging, Aichi Medical University, 1-1 Yazakokarimata, Nagakute, Aichi, 480-1195, Japan.
James K ChambersLaboratory of Veterinary Pathology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Riki KoikeLaboratory for Alzheimer's Disease, Department of Life Science, Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo, 171-8588, Japan.
Moniruzzaman MohammadDepartment of Diagnostics and Therapeutics for Brain Disease, Molecular Neuroscience Research Center, Shiga University of Medical Science, Seta Tsukinowa-cho, Otsu, Shiga, 520-2192, Japan.
Akihiko TakashimaLaboratory for Alzheimer's Disease, Department of Life Science, Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo, 171-8588, Japan.

Funding

Japan Agency for Medical Research and Development (AMED) JP21wm0425016MEXT | Japan Society for the Promotion of Science (JSPS) 20K06896MEXT | Japan Society for the Promotion of Science (JSPS) 23K05993
6 · The paper itself

Abstract

Prior to the formation of amyloid fibrils, the pathological hallmark in tau-related neurodegenerative disease, tau monomers aggregate into a diverse range of oligomers. Granular tau oligomers, consisting of approximately 40 tau protein molecules, are present in the prefrontal cortex of patients at Braak stages I-II, preclinical stages of Alzheimer's disease (AD). Antibodies to granular tau oligomers as antigens have not been reported. Therefore, we generated new rat monoclonal antibodies by immunization with granular tau oligomers. Three antibodies from different hybridoma clones showed stronger immunoreactivity to granular tau oligomers and tau fibrils compared with monomeric tau. Of the three antibodies, 2D6-2C6 showed 3000-fold greater immunoreactivity in P301L-tau transgenic (rTg4510) mice than in non-transgenic mice, while MC1 antibody, which detects pathological conformations of tau, showed a 5.5-fold increase. These results suggest that 2D6-2C6 recognizes aggregates more specifically than MC1. In AD subjects, 2D6-2C6 recognized neurofibrillary tangles and pretangles, and co-localized within AT8-positive cells containing phosphorylated tau aggregates. The epitope of 2D6-2C6 is the 423-430 amino acid (AA) sequence of C-terminal regions. Taken together, a novel monoclonal antibody, 2D6-2C6, generated by immunization with granular tau oligomers binds to tau aggregates at the 423-430 AA sequence.

Indexed as

Alzheimer DiseaseAntibodies, MonoclonalMice, Transgenictau ProteinsAgedAmino Acid SequenceAnimalsEpitopesFemaleHumansImmunizationMaleMiceNeurofibrillary TanglesProtein AggregatesRatsAntibodies, MonoclonalEpitopesProtein Aggregatestau ProteinsAntibodyC-terminal regions of tauGranular tau oligomersTau aggregation

Identifiers

PMID39060263
PMCPMC11282240

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.