Cloning and characterization of an inhibitor of apoptosis protein (IAP) from Bombyx mori

Q. Huang, Q. L. Deveraux, S. Maeda, H. R. Stennicke, B. D. Hammock, J. C. Reed

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


We cloned a novel inhibitor of apoptosis protein (IAP) family member, BmIAP, from Bombyx mori BmN cells. BmIAP contains two baculoviral IAP repeat (BIR) domains followed by a RING domain. BmIAP shares striking amino acid sequence similarity with lepidopteran IAPs, SfIAP and TnIAP, and with two baculoviral IAPs, CpIAP and OpIAP, suggesting evolutionary conservation. BmIAP blocks programmed cell death (apoptosis) in Spodoptera frugiperda Sf-21 cells induced by p35 deficient Autographa californica nucleopolyhedrovirus (AcMNPV). This anti-apoptotic function requires both the BIR domains and RING domain of BmIAP. In mammalian cells, BmIAP inhibits Bax induced but not Fas induced apoptosis. Further biochemical data suggest that BmIAP is a specific inhibitor of mammalian caspase-9, an initiator caspase in the mitochondria/cytochrome-c pathway, but not the downstream effector proteases, caspase-3 and caspase-7. These results suggest that suppression of apoptosis by lepidopteran IAPs in insect cells may involve inhibition of an upstream initiator caspase in the conserved mitochondria/cytochrome-c pathway for apoptosis.

Original languageEnglish (US)
Pages (from-to)191-198
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number3
StatePublished - Jan 15 2001
Externally publishedYes


  • Apoptosis
  • Caspase
  • Cell death
  • Inhibitor of apoptosis protein
  • Insect
  • Protease inhibitor

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Biophysics


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