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Antibody cross-reactivity with CD46 and lack of cell surface expression suggest that moesin might not mediate measles
1Immunité et Infections Virales, IVMC, CNRS-UCBL UMR 5537, Faculté de Médecine Lyon RTH Laënnec, France.
Abstract:
The binding of antimoesin antibodies from ascites fluids to the surfaces of human and rodent cells was found to parallel the level of CD46 expression. No such reactivity was detected with a purified antimoesin antibody which recognized intracellular moesin. In Western blots, antimoesin antibodies were found to react with solubilized CD46 and a recombinant soluble form of CD46. Antimoesin antibodies also reacted with CD46/CD4 molecules containing only the SCR I and II domains required for measles virus (MV) hemagglutinin binding onto CD46. We suggest that the weak cross-reactivity of antimoesin antibodies with CD46 explains the inhibitory effect of these antibodies on MV entry and that moesin is not directly involved in MV binding.
Insights
Antimoesin antibodies bind to cells expressing CD46, inhibiting measles virus entry. This binding is due to cross-reactivity with CD46, not direct interaction with moesin.
Area of Science:
- Immunology
- Virology
- Cell Biology
Background:
- CD46 is a cell surface receptor involved in immune regulation and serves as a receptor for measles virus (MV).
- Moesin is a protein involved in cell structure and signaling, and its potential role in MV entry has been investigated.
Purpose of the Study:
- To investigate the interaction between antimoesin antibodies, CD46, and measles virus entry.
- To determine if moesin is directly involved in measles virus binding to CD46.
Main Methods:
- Cell surface binding assays using antimoesin antibodies and human/rodent cells with varying CD46 expression levels.
- Western blot analysis of antimoesin antibody reactivity with purified CD46 and CD46 domains.
- Testing the effect of antimoesin antibodies on measles virus entry.
Main Results:
- Antimoesin antibodies from ascites fluids bound to cells in parallel with CD46 expression.
- Purified antimoesin antibodies recognizing intracellular moesin did not show cell surface reactivity.
- Antimoesin antibodies reacted with solubilized CD46 and CD46 domains essential for MV binding.
- These antibodies showed weak cross-reactivity with CD46, explaining their inhibitory effect on MV entry.
Conclusions:
- The inhibitory effect of antimoesin antibodies on measles virus entry is attributed to their weak cross-reactivity with CD46.
- Moesin is not directly involved in the binding of measles virus to CD46.