C3b 2026-11-05
C3b is a large activated fragment produced by proteolysis of Complement C3. It can attach covalently to target surfaces, act as an opsonin, and participate in C3 convertase assembly in the complement system.[ref]
Structure of complement fragment C3b-factor H and implications for host protection by complement regulators by Jin Wu and others. Introduction and Results: C3b formation, surface attachment and regulatory interactions
Processing changes its functions. Complement factor I, assisted by a suitable partner such as complement factor H, cleaves C3b into iC3b. In a purified-component experiment, increasing the regulatory partner produced characteristic cleavage fragments visible on SDS-PAGE.[ref]
Think of two distinct experimental measurements: a surface assay detects deposited C3b, while an activity assay tests further complement system amplification. Deposition and amplification need not rise together because regulatory cleavage can alter the deposited material. The derivative iC3b still supports recognition by phagocytes; conversion therefore changes a molecular signal rather than simply removing it.[ref]
iC3b 2026-11-05
iC3b is a processed fragment of C3b formed through cleavage by complement factor I with a suitable partner such as complement factor H. It functions as an opsonin: deposition on a target supports recognition and uptake by phagocytes, including through complement receptor 3. [ref]
https://pmc.ncbi.nlm.nih.gov/articles/PMC9005620/. 2022 original iC3b–CR3 structure paper, Introduction: C3b processing and opsonin recognition
Processing does not simply erase every biological effect of the original protein. It changes the interactions available to the resulting fragment. In a 1983 experiment, cultured monocytes on appropriately coated surfaces showed complement-associated phagocytosis without the appreciable hydrogen peroxide release seen with the IgG-coated comparison.[ref]
The comparison separates target uptake from an oxidative response. Measuring either alone would miss that separation; receptor engagement, ingestion and production of reactive substances are distinct experimental readouts. The older paper writes the fragment as C3bi; iC3b is the corresponding modern notation.
Opsonin 2026-11-05
An opsonin is a substance that coats a target and promotes recognition and uptake by a phagocyte. The name describes a biological role: IgG and complement system fragments such as C3b and iC3b can supply different molecular handles for phagocytosis.[ref]
Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes by S. D. Wright and S. C. Silverstein. Introduction: recognition of coated particles by complement and Fc receptors
A 1983 experiment separated uptake from another response. Cultured monocytes in contact with appropriate fibronectin-containing surfaces could ingest complement-coated targets without the substantial hydrogen peroxide release seen in the IgG comparison.[ref]
Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes by S. D. Wright and S. C. Silverstein. Abstract and Figure 1: uptake and oxidative-response comparisons
Thus, coating, receptor engagement, phagocytosis and oxidant production are distinguishable steps. Calling a protein an opsonin does not imply that it digests the target itself, or that every receptor-triggered response accompanies uptake. A useful assay measures binding and internalization separately: a particle attached to a cell membrane is not necessarily inside the biological cell.