# The fixation of complement protein pairs to CR2 isoforms

**Authors:** Giuseppe Barile

PMC · DOI: 10.1016/j.bbrep.2024.101657 · Biochemistry and Biophysics Reports · 2024-02-10

## TL;DR

The study explores how complement proteins bind to CR2 isoforms and how low molecular weight molecules are released during this process.

## Contribution

The paper identifies the release of low molecular weight molecules from C3d during fixation to CR2 and their potential role in protein binding.

## Key findings

- Low molecular weight molecules are released when i-C3 and C3b bind to CR2 isoforms.
- Aromatic residues in C3c differ from those in C3d, possibly affecting fixation processes.

## Abstract

Reviewing old protocols, it was found that Raji, a CR2-posistive cell line, binds both endogenous (e-C3) and exogenous C3 (i-C3). The processing of i-C3 to an i-C3b-like protein and their fixation to CR2 isoforms resulted in the formation of heterodimers whose units might be linked via thioester by low m.w. molecule(s). In an attempt to study the origin of the low m.w. molecules, it was found that they were detected following I12⁵-C3d treatment with NHS or hi-S. Indirect evidence would suggest that the products of C3 fragment fixation could have a short half-life and that the aromatic residues present in C3d might have different physico-chemical characteristics than those present in C3c. The surface hydrophobicity expressed by these aromatic residues could be required for the fixation of C3 or CR2 fragments to cell surface proteins.

•Low mw molecules are released following the fixation of i-C3 and C3b to CR2 isoforms.•They are released from the C3d component of CR2 complex or of CR2 ligands.•Low m.w. molecules can therefore have both endogenous and exogenous origins.•Aromatic residues present in C3c have different features than those present in C3d.•Their hydrophobicity may then be necessary for the fixation of C3 or CR2 fragments.

Low mw molecules are released following the fixation of i-C3 and C3b to CR2 isoforms.

They are released from the C3d component of CR2 complex or of CR2 ligands.

Low m.w. molecules can therefore have both endogenous and exogenous origins.

Aromatic residues present in C3c have different features than those present in C3d.

Their hydrophobicity may then be necessary for the fixation of C3 or CR2 fragments.

## Linked entities

- **Proteins:** CR2 (complement C3d receptor 2), C3 (complement C3), C3 (complement C3), ERVK-13 (endogenous retrovirus group K member 13), Or4c58 (olfactory receptor family 4 subfamily C member 58), ewg (erect wing)

## Full-text entities

- **Genes:** ERVK-13 (endogenous retrovirus group K member 13) [NCBI Gene 100861467] {aka c3_D}
- **Chemicals:** hi-S. (MESH:D006639)
- **Cell lines:** Raji — Homo sapiens (Human), EBV-related Burkitt lymphoma, Cancer cell line (CVCL_0511)

## Full text

_Full body text omitted from this summary view._ Fetch the complete paper as Markdown: https://tomesphere.com/paper/PMC10869749/full.md

## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC10869749/full.md

## References

31 references — full list in the complete paper: https://tomesphere.com/paper/PMC10869749/full.md

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Source: https://tomesphere.com/paper/PMC10869749