The structure of the mouse lymphocyte pore-forming protein perforin

Byoung S. Kwon*, Mark Wakulchik, Chau Ching Liu, Pedro M. Persechini, Joseph A. Trapani, Asifa K. Haq, Yeong Kim, John Ding E. Young

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

60 Scopus citations


Purified murine lymphocyte pore-forming protein (PFP or perforin) was partially sequenced. Oligonucleotides synthesized on the basis of this sequence information were used to screen a murine cytotoxic T lymphocyte (CTL) cDNA library. Seven clones were obtained, two of which were sequenced, providing full-length sequence information on PFP. Murine PFP (534 a.a.) is 68% identical to human PFP. Hydropathic analysis revealed a predominantly hydrophilic protein with some hydrophobic domains, including a region (a.a. 191-251) that could contain putative membrane-spanning domains. PFP is approx. 20% identical to human C7, C8 and C9 within a region encompassing 270 a.a., confirming previous immunological cross-reactivity studies. Northern blot analysis showed that expression of PFP but not of a serine esterase transcript is enhanced in a CTL line by antigen receptor-stimulation. Southern blot analysis of mouse genomic DNA indicated that PFP is encoded as a single-copy gene with the coding region contained within 10 kilobases of genomic DNA.

Original languageEnglish
Pages (from-to)1-10
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 16 01 1989
Externally publishedYes


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