Structural characterization and comparative modeling of PD-Ls 1-3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L.

Antimo Di Maro, Angela Chambery, Vincenzo Carafa, Susan Costantini, Giovanni Colonna, Augusto Parente

Research output: Contribution to journalArticlepeer-review

Abstract

The amino acid sequence and glycan structure of PD-L1, PD-L2 and PD-L3, type 1 ribosome-inactivating proteins isolated from Phytolacca dioica L. leaves, were determined using a combined approach based on peptide mapping, Edman degradation and ESI-Q-TOF MS in precursor ion discovery mode. The comparative analysis of the 261 amino acid residue sequences showed that PD-L1 and PD-L2 have identical primary structure, as it is the case of PD-L3 and PD-L4. Furthermore, the primary structure of PD-Ls 1-2 and PD-Ls 3-4 have 81.6% identity (85.1% similarity). The ESI-Q-TOF MS analysis confirmed that PD-Ls 1-3 were glycosylated at different sites. In particular, PD-L1 contained three glycidic chains with the well known paucidomannosidic structure (Man) 3 (GlcNAc) 2 (Fuc) 1 (Xyl) 1 linked to Asn10, Asn43 and Asn255. PD-L2 was glycosylated at Asn10 and Asn43, and PD-L3 was glycosylated only at Asn10. PD-L4 was confirmed to be not glycosylated. Despite an overall high structural similarity, the comparative modeling of PD-L1, PD-L2, PD-L3 and PD-L4 has shown potential influences of the glycidic chains on their adenine polynucleotide glycosylase activity on different substrates.

Original languageEnglish
Pages (from-to)352-363
Number of pages12
JournalBiochimie
Volume91
Issue number3
DOIs
Publication statusPublished - Mar 2009

Keywords

  • Comparative modeling
  • Edman degradation
  • ESI-Q-TOF mass spectrometry
  • Phytolacca dioica
  • Ribosome-inactivating proteins

ASJC Scopus subject areas

  • Biochemistry

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