Rapid degradation of the complement regulator, CD59, by a novel inhibitor

Bishuang Cai, Shuwei Xie, Fengming Liu, Laura C. Simone, Steven H Caplan, Xuebin Qin, Naava Naslavsky

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Background: Surface expression of complement inhibitors, such as the glycosylphosphatidylinositol-anchored protein CD59, prevent complement-dependent lysis of cancer cells. Results: The non-toxic domain-4 of the bacterial toxin intermedilysin (rILYd4) blocks CD59 complement inhibitory activity. Conclusion: rILYd4 induces CD59 internalization and rapid degradation in lysosomes in non-small lung carcinoma cells. Significance: CD59 serves as a model for glycosylphosphatidylinositol-anchored protein trafficking and rILYd4 shows potential for immunotherapy.

Original languageEnglish (US)
Pages (from-to)12109-12125
Number of pages17
JournalJournal of Biological Chemistry
Volume289
Issue number17
DOIs
StatePublished - Apr 25 2014

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Glycosylphosphatidylinositols
Complement Inactivating Agents
Cells
Bacterial Toxins
Degradation
Protein Transport
Lysosomes
Non-Small Cell Lung Carcinoma
Immunotherapy
Proteins
Neoplasms
Streptococcus intermedius intermedilysin protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Rapid degradation of the complement regulator, CD59, by a novel inhibitor. / Cai, Bishuang; Xie, Shuwei; Liu, Fengming; Simone, Laura C.; Caplan, Steven H; Qin, Xuebin; Naslavsky, Naava.

In: Journal of Biological Chemistry, Vol. 289, No. 17, 25.04.2014, p. 12109-12125.

Research output: Contribution to journalArticle

Cai, Bishuang ; Xie, Shuwei ; Liu, Fengming ; Simone, Laura C. ; Caplan, Steven H ; Qin, Xuebin ; Naslavsky, Naava. / Rapid degradation of the complement regulator, CD59, by a novel inhibitor. In: Journal of Biological Chemistry. 2014 ; Vol. 289, No. 17. pp. 12109-12125.
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