Calcium Modulation of Monoclonal Antibody Binding to Phosphatidylinositol Phosphate.
From: Henry M. Jackson Foundation for Military Medical Research, USA.
Biochemical and biophysical research communications
- Publish Date: Mar 2007
- ISSN: 0006-291X
- Volume: 354
- Issue: 3
- Pages: 747-51
- Medium: Print
- Language: English
- Citation (JAMA): Beck Zoltan, Karasavvas Nicos, Tong James, et al. Calcium Modulation of Monoclonal Antibody Binding to Phosphatidylinositol Phosphate.. Biochem. Biophys. Res. Commun. Mar 2007;354:747-51
Abstract
The binding characteristics of two monoclonal antibodies (mAb) to phosphatidylinositol-4-phosphate (PIP) were examined: a murine IgM mAb to PIP; and a human IgG mAb (4E10) that binds both to HIV-1 envelope protein and also to neutral and anionic phospholipids, including PIP. Binding of each mAb to pure PIP was inhibited by Ca(2+) as determined by ELISA. When studied by surface plasmon resonance, liposomes containing PIP could be stripped (i.e., removed) by either Ca(2+) or phosphorylated haptens after binding of the liposomes to the murine anti-PIP antibody attached to a BIAcore chip. In contrast, the binding of liposomal PIP to 4E10 was irreversible and could not be stripped. We therefore conclude that Ca(2+) and phosphate can modulate the initial binding of both types of antibodies to PIP. However, 4E10 binds to liposomal PIP in a two-stage process involving first Ca(2+)-modulated binding to the PIP polar headgroup, followed by irreversible binding to liposomal hydrophobic groups.
Mesh Headings (Keywords): Animals, Antibodies, Monoclonal, Binding Sites, Calcium, Cations, Divalent, Dose-Response Relationship, Drug, Edetic Acid, Enzyme-Linked Immunosorbent Assay, HIV-1, Humans, Hydrophobicity, Immunoglobulin M, Liposomes, Mice, Phosphatidylinositol Phosphates, Phospholipids, Viral Envelope Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 17257584
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