Human LilrB2 Is a β-Amyloid Receptor and Its Murine Homolog PirB Regulates Synaptic Plasticity in an Alzheimer’s Model
Open accessAbstract
Amyloid Binding Partners: Amyloid-β (Aβ) is critical to the pathology of Alzheimer's disease (AD), but its role in normal physiology remains unclear. Kim et al. (p. 1399 ; see the Perspective by Benilova and De Strooper ) found that murine-paired immunoglobulin-like receptor B (PirB) and its human ortholog, leukocyte immunoglobulin-like receptor B2 (LilrB2) both bound to oligomerized Aβ. Early in mouse development, ocular dominance plasticity was affected by interactions between oligomeric Aβ and PirB. In hippocampal brain slices from a mouse model of AD, reductions in long-term potentiation induced by Aβ required PirB. Furthermore, the memory defects characteristic of a mouse model of AD were dependent on function of PirB. Many binding partners for Aβ have been identified, and so the extent to which these findings can be exploited therapeutically remains unclear.
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Amyloid proteins can regulate immune responses by interacting with different immune receptors.
“Researches revealed that amyloid proteins can regulate immune responses by interacting with different immune receptors.”
From Oligomeric cystatin C supports the immunosuppressive activity of myeloid cells through interaction with inhibitory receptors (2025) · cites this paper as [3]
The paper’s Abstract (page unavailable in our copy) reports that β-amyloid oligomers bind PirB and LilrB2, receptors associated with the immune system. It links that interaction to synaptic loss and impaired plasticity, not to regulation of immune responses. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAmyloid β interacts with immune inhibitory receptors, leading to suppression of immune cell activity.
“Conversely, Aβ has also been reported to interact with immune inhibitory receptors, leading to suppression of immune cell activity and highlighting its context-dependent immunomodulatory capacity3.”
From Oligomeric cystatin C supports the immunosuppressive activity of myeloid cells through interaction with inhibitory receptors (2025) · cites this paper as [3]
The indexed paper reports that Aβ oligomers bind PirB and LilrB2, receptors associated with inhibitory signaling in the immune system. Its reported consequences of Aβ binding concern neuronal signaling and synaptic plasticity, not suppression of immune cell activity. The passages are indexed under “Abstract”; no page number is provided. (LLM, conf=0.90)
Experimental — accuracy not yet measuredSIGLEC11 and LILRB2 have already been linked to Aβ peptides/amyloid plaques.
“Importantly, SIGLEC11 and LILRB2 have already been linked to Aβ peptides/amyloid plaques25,26.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [25]
Binding between oAβ and PirB recruits cofilin-signaling modules, leading to actin depolymerization, resulting in synaptic dysfunction and cognitive deficits.
“Therefore, binding between oAβ and PirB would recruit cofilin-signaling modules, which leads to actin depolymerization, resulting in synaptic dysfunction and cognitive deficits [93].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [93]
Deletion of PirB rescued hippocampal LTP deficits induced by Aβ42 oligomers.
“Deletion of PirB rescued hippocampal LTP deficits induced by Aβ42 oligomers.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [93]
Human LilrB2 and its murine homolog PirB are potential oAβ receptors.
“A recent study has linked LilrB2 to AD, and suggests that human LilrB2 and its murine homolog paired immunoglobulin-like receptor B (PirB) are potential oAβ receptors [93].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [93]
PirB interacts with cofilin, and levels of the inactive phosphorylated form of cofilin in human AD brains appear to be reduced.
“Mechanistically, PirB interacts with cofilin, and levels of the inactive phosphorylated form of cofilin in human AD brains appear to be reduced.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [93]
PirB deficiency can rescue cognitive deficits in an AD mouse model.
“In addition, PirB deficiency can rescue cognitive deficits in an AD mouse model.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [93]
LILRB2 and its mouse orthologue Pirb bind Aβ, and this interaction with Aβ in mice mediates synapse elimination, and deficits in synaptic plasticity and memory.
“A paralogue of LILRB4, named LILRB2, and its mouse orthologue Pirb have been shown to bind Aβ, and this interaction with Aβ in mice mediates synapse elimination, and deficits in synaptic plasticity and memory (Kim et al., 2013).”
From Genetic variability in response to amyloid beta deposition influences Alzheimer’s disease risk (2019) · cites this paper as Kim et al., 2013
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- Authors
- Kim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., & Shatz, C. J.
- Affiliations
- Stanford University (US)
- Massachusetts General Hospital (US)
- Howard Hughes Medical Institute (US)
- Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, and Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
- Corresponding author
- Kim, Taeho
- Shatz, Carla J.
- ORCID
- Venue
- Science
- Published
- 2013-09-20
- Volume
- 341
- Issue
- 6152
- Pages
- 1399-1404
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3853120
- OpenAlex
- W1965552543
- Cited by
- 410
- References
- 49
- Citations by year
- 2026: 21 · 2025: 20 · 2024: 37 · 2023: 21 · 2022: 41 · 2021: 41 · 2020: 24 · 2019: 28 · 2018: 24 · 2017: 34 · 2016: 40 · 2015: 39 · 2014: 32 · 2013: 8
- FWCI
- 27.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute on Aging (R01AG041507, P50AG005134, P30AG062421)
- National Institute of Mental Health (R01MH071666, T32MH020016)
- National Eye Institute (T32EY020485, EY02858, R01EY002858, R37EY002858)
- National Institute of Neurological Disorders and Stroke (NS069375, P30NS069375, K08NS069811)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- LILRB2, PirB, amyloid-beta oligomers, Alzheimer's disease, synaptic plasticity, immunoglobulin domains, long-term potentiation, hippocampus, visual cortex, memory impairment, transgenic mouse model, receptor binding affinity
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Female, Hippocampus, Humans, Male, Membrane Glycoproteins, Mice, Transgenic, Neuronal Plasticity, Peptide Fragments, Receptors, Immunologic, Synapses, Amyloid beta-Peptides, Long-Term Potentiation, Mice, HEK293 Cells
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