Antibody cross-reactivity with CD46 and lack of cell surface expression suggest that moesin might not mediate measles virus binding

Patricia Devaux, D. Gerlier

Research output: Contribution to journalArticle

8 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1679-1682
Number of pages4
JournalJournal of Virology
Volume71
Issue number2
StatePublished - 1997
Externally publishedYes

Fingerprint

Measles virus
Virus Attachment
cross reaction
antibodies
Antibodies
cells
Virus Internalization
CD4 Antigens
ascites
Hemagglutinins
hemagglutinins
Ascites
moesin
Rodentia
Western blotting
rodents
Western Blotting

ASJC Scopus subject areas

  • Immunology

Cite this

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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.",
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journal = "Journal of Virology",
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T1 - Antibody cross-reactivity with CD46 and lack of cell surface expression suggest that moesin might not mediate measles virus binding

AU - Devaux, Patricia

AU - Gerlier, D.

PY - 1997

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AB - 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.

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