The ninth component of complement and the pore-forming protein (perforin 1) from cytotoxic T cells: Structural, immunological, and functional similarities

John Ding E. Young*, Zanvil A. Cohn, Eckhard R. Podack

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

228 Scopus citations

Abstract

The ninth component of complement (C9) and the pore-forming protein (PFP or perform) from cytotoxic T lymphocytes polymerize to tubular lesions having an internal diameter of 100 Å and 160 Å, respectively, when bound to lipid bilayers. Polymerized C9, assembled by slow spontaneous or rapid Zn 2+-induced polymerization, and polyperforin, which is assembled only in the presence of Ca2+, constitute large aqueous pores that are stable, nonselective for solutes, and insensitive to changes of membrane potential. Monospecific potydonal antibodies to purified C9 and PFP show cross-reactivity, suggesting structural homology between the two molecules. The structural and functional homologies between these two killer molecules imply an active role for pore formation during cell lysis.

Original languageEnglish
Pages (from-to)184-190
Number of pages7
JournalScience
Volume233
Issue number4760
DOIs
StatePublished - 1986
Externally publishedYes

Keywords

  • Animal
  • Centrifugation, Isopycnic
  • Complement 9
  • Cross Reactions
  • Human
  • Ion Channels
  • Membrane Proteins
  • Mice
  • Molecular Weight
  • Support, Non-U.S. Gov't
  • Support, U.S. Gov't, P.H.S.
  • T-Lymphocytes, Cytotoxic
  • Zinc

Fingerprint

Dive into the research topics of 'The ninth component of complement and the pore-forming protein (perforin 1) from cytotoxic T cells: Structural, immunological, and functional similarities'. Together they form a unique fingerprint.

Cite this