# Chimerolectins: Classification, structural architecture, and functional perspectives

**Authors:** Vanir Reis Pinto‐Junior, Benildo Sousa Cavada, Kyria Santiago Nascimento

PMC · DOI: 10.1002/pro.70261 · 2025-08-15

## TL;DR

Chimerolectins are versatile proteins combining lectin domains with other functional domains, playing roles in immunity, disease, and biotechnology.

## Contribution

The paper provides a comprehensive overview of chimerolectins, their structural features, and their functional roles across different biological contexts.

## Key findings

- Chimerolectins expand lectin functionality by combining with enzymatic or signaling domains.
- They are involved in immune regulation, plant defense, and disease pathogenesis.
- Structural insights have enabled the development of antiviral chimerolectins and cancer-targeting therapies.

## Abstract

Lectins are proteins or glycoproteins capable of binding specifically and reversibly to carbohydrates, a property that, in itself, gives them great functional versatility in organisms from all kingdoms of nature. A subclass of these proteins, called chimerolectins, is composed of proteins that have at least one lectin domain associated with another functional domain, such as enzymatic domains or modules involved in molecular signaling processes. The emergence of chimerolectins throughout evolution significantly expanded the functional repertoire of lectins, allowing their action to go beyond the interaction with carbohydrates and glycoconjugates. These proteins are involved in the regulation of the immune system in humans and animals, in the defense of plants against pathogens and predators, as well as in the mediation of responses to biotic and abiotic stresses. In addition, they can act as potent lethal toxins or as factors in the infection of several pathogens and are often associated with the manifestation of symptoms of diseases, which makes them therapeutic targets of great interest. Deepening the structural knowledge of these proteins has been essential for understanding their mechanisms of action, in addition to providing solid bases for biotechnological applications and for the rational development of artificial lectins with specific functions. This approach has enabled the creation of chimerolectins with potent antiviral activity, as well as the development of new therapeutic strategies aimed at inducing death in cells of different tumor lineages.

## Full-text entities

- **Genes:** ITIH4 (inter-alpha-trypsin inhibitor heavy chain 4) [NCBI Gene 3700] {aka GP120, H4P, IHRP, ITI-HC4, ITIHL1, PK-120}, MBL2 (mannose binding lectin 2) [NCBI Gene 4153] {aka COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C}, ASGR1 (asialoglycoprotein receptor 1) [NCBI Gene 432] {aka ASGPR, ASGPR1, CLEC4H1, HL-1}, CLEC4F (C-type lectin domain family 4 member F) [NCBI Gene 165530] {aka CLECSF13, KCLR, KCR}, SIGLEC5 (sialic acid binding Ig like lectin 5) [NCBI Gene 8778] {aka CD170, CD33L2, OB-BP2, OBBP2, SIGLEC-5}, TLR4 (toll like receptor 4) [NCBI Gene 7099] {aka ARMD10, CD284, TLR-4, TOLL}, HCST (hematopoietic cell signal transducer) [NCBI Gene 10870] {aka DAP10, KAP10, PIK3AP}, SKP1 (S-phase kinase associated protein 1) [NCBI Gene 6500] {aka EMC19, OCP-II, OCP2, SKP1A, TCEB1L, p19A}, RPGR (retinitis pigmentosa GTPase regulator) [NCBI Gene 6103] {aka COD1, CORDX1, CRD, PCDX, RP15, RP3}, FN1 (fibronectin 1) [NCBI Gene 2335] {aka CIG, ED-B, FINC, FN, FNZ, GFND}, PTPN11 (protein tyrosine phosphatase non-receptor type 11) [NCBI Gene 5781] {aka BPTP3, CFC, JMML, METCDS, NS1, PTP-1D}, SIGLEC1 (sialic acid binding Ig like lectin 1) [NCBI Gene 6614] {aka CD169, SIGLEC-1, SN}, LGALS3 (galectin 3) [NCBI Gene 3958] {aka CBP35, GAL3, GALBP, GALIG, L31, LGALS2}, TYROBP (transmembrane immune signaling adaptor TYROBP) [NCBI Gene 7305] {aka DAP12, KARAP, PLOSL, PLOSL1}, KITLG (KIT ligand) [NCBI Gene 4254] {aka DCUA, DFNA69, FPH2, FPHH, KL-1, Kitl}, MASP1 (MBL associated serine protease 1) [NCBI Gene 5648] {aka 3MC1, CRARF, CRARF1, MAP-1, MAP1, MASP}, CD209 (CD209 molecule) [NCBI Gene 30835] {aka CDSIGN, CLEC4L, DC-SIGN, DC-SIGN1, hDC-SIGN}, NR0B2 (nuclear receptor subfamily 0 group B member 2) [NCBI Gene 8431] {aka SHP, SHP1}, BCL2 (BCL2 apoptosis regulator) [NCBI Gene 596] {aka Bcl-2, PPP1R50}, CACUL1 (CDK2 associated cullin domain 1) [NCBI Gene 143384] {aka C10orf46, CAC1}, Ricin [NCBI Gene 8261245]
- **Diseases:** SYNTHETIC (OMIM:146820), LECTINS (MESH:C563602), inflammation (MESH:D007249), cytotoxic (MESH:D064420), infection (MESH:D007239), viral infections (MESH:D014777), cancer (MESH:D009369), pancreatic, colon, and stomach tumor (MESH:D010190), ND (OMIM:300855), vascular damage (MESH:D057772), lymphoma (MESH:D008223)
- **Chemicals:** fucose (MESH:D005643), Sialic acid (MESH:D019158), chitin (MESH:D002686), Tyr (MESH:D014443), carbohydrate (MESH:D002241), ATP (MESH:D000255), N-acetyl-D-glucosamine (MESH:D000117), N-acetylgalactosamine (MESH:D000116), D-galactose (MESH:D005690), glycolipids (MESH:D006017), manganese (MESH:D008345), hydrogen (MESH:D006859), lactose (MESH:D007785), globotriaosylceramide (MESH:C018549), trisaccharide (MESH:D014312), Trp (MESH:D014364), amino acids (MESH:D000596), D-mannose (MESH:D008358), lipid (MESH:D008055), water (MESH:D014867), glycan (MESH:D011134), N-acetyllactosamine (MESH:C000458), copper (MESH:D003300), galactosides (MESH:D005697), metal (MESH:D008670), hydrogen peroxide (MESH:D006861), glucose (MESH:D005947), 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (MESH:C036137), monosaccharide (MESH:D009005), oligosaccharides (MESH:D009844), adenine (MESH:D000225), Gal1 (MESH:C012614), sugar (MESH:D000073893), Asn (MESH:D001216), Man3-9GlcNAc2 (-), calcium (MESH:D002118), aldehyde (MESH:D000447), polylactosamines (MESH:C066929)
- **Species:** Tetranychus urticae (red spider mite, species) [taxon 32264], Burkholderia cenocepacia (species) [taxon 95486], Human immunodeficiency virus 1 (no rank) [taxon 11676], Aeromonas (genus) [taxon 642], Simarouba glauca (aceituno, species) [taxon 43729], Escherichia coli (E. coli, species) [taxon 562], Severe acute respiratory syndrome coronavirus 2 (no rank) [taxon 2697049], Lablab purpureus (antaque, species) [taxon 35936], Micromonospora viridifaciens (species) [taxon 1881], Homo sapiens (human, species) [taxon 9606], Streptococcus pneumoniae (species) [taxon 1313], Griffithsia sp. (species) [taxon 2877960], Parkia platycephala (species) [taxon 185447], Tamarindus indica (tamarind, species) [taxon 58860], Hevea brasiliensis (jebe, species) [taxon 3981], Ricinus communis (castor bean, species) [taxon 3988], Pseudomonas aeruginosa (species) [taxon 287], Scytonema varium (species) [taxon 423208], Amaranthus caudatus (amaranth, species) [taxon 3567], Vibrio cholerae (species) [taxon 666], Canavalia ensiformis (horse bean, species) [taxon 3823], Fusarium sp. (species) [taxon 29916], Clostridium perfringens (species) [taxon 1502], Shigella dysenteriae (species) [taxon 622]
- **Mutations:** Ser/Thr, H84T, glutamic acid amino acid at position 167
- **Cell lines:** DLL-II — Mus musculus (Mouse), Hybridoma (CVCL_B3SP)

## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12355970/full.md

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Source: https://tomesphere.com/paper/PMC12355970