Molecular basis of fibrinogen recognition by the innate immune receptor LILRA2.

Jiaqi Wang, Atsushi Furukawa, Liuan Chen, Ryo Suzuki, Hisashi Arase, Kouyuki Hirayasu, Katsumi Maenaka

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 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

7 authors.

Jiaqi WangLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

Atsushi FurukawaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan; Faculty of Pharmaceutical Sciences, Institute of Medical, Pharmaceutical and Health Sciences, Kanazawa University, Kanazawa, Japan. Electronic address: afuru@p.kanazawa-u.ac.jp.

Liuan ChenLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

Ryo SuzukiFaculty of Pharmaceutical Sciences, Institute of Medical, Pharmaceutical and Health Sciences, Kanazawa University, Kanazawa, Japan.

Hisashi AraseDepartment of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Suita, Japan; WPI Immunology Frontier Research Center, Osaka University, Suita, Japan; Center for Advanced Modalities and DDS, Osaka University, Osaka, Japan; Center for Infectious Disease Education and Research, Osaka University, Osaka, Japan.

Kouyuki HirayasuAdvanced Preventive Medical Sciences Research Center, Kanazawa University, Kanazawa, Ishikawa, Japan.

Katsumi MaenakaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan; Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan; Global Station for Biosurfaces and Drug Discovery, Hokkaido University, Sapporo, Japan; Hokkaido University Institute for Vaccine Research & Development, Sapporo, Japan; Faculty of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan. Electronic address: maenaka@pharm.hokudai.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human leukocyte immunoglobulin-like receptors (LILRs) are cell surface receptors that are mainly expressed in immune cells. LILRs are involved in immune cell regulation. As a member of the LILR family, LILRA2 was reported to recognize the bacterially N-terminus truncated Ig (N-truncated Ig) for the induction of innate immune response. Fibrinogen, which is enzymatically converted to fibrin and forms fibrin-based blood clots, was recently shown to activate LILRA2-expressing immune cells. However, the molecular mechanisms of LILRA2-fibrinogen interaction remain unclear. In this study, we investigated the molecular recognition of fibrinogen by LILRA2, using biophysical methods. Surface plasmon resonance (SPR) analysis showed that LILRA2 specifically bound to fibrinogen with a relatively low dissociation constant (K

Indexed as

FibrinogenImmunity, InnateReceptors, ImmunologicHumansInnate Immunity RecognitionProtein BindingSurface Plasmon ResonanceFibrinogenReceptors, Immunologicbiophysical analysiscell surface receptorfibrinogenimmunologypaired-type receptor

Identifiers

PMID41690595

DOI10.1016/j.jbc.2026.111276

PMCPMC12995826

What Socratic holds

Textmetadata

LicenceCC BY-NC-ND

Read underepoch 390

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 Socratic graph.