PmST2: A novel Pasteurella multocida glycolipid α2-3- sialyltransferase

Vireak Thon, Kam Lau, Hai Yu, Bao K. Tran, Xi Chen

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Pasteurella multocida (Pm) is a multi-species pathogen that causes diseases in animals and humans. Sialyltransferase activity has been detected in multiple Pm strains and sialylation has been shown to be important for the pathogenesis of Pm. Three putative sialyltransferase genes have been identified in Pm genomic strain Pm70. We have reported previously that a Pm0188 gene homolog in Pm strain P-1059 (ATCC 15742) encodes a multifunctional sialyltransferase (PmST1). We demonstrate here that while PmST1 prefers to use oligosaccharides as acceptors, PmST2 encoded by the Pm0508 gene homolog in the same Pm strain is a novel glycolipid α2-3-sialyltransferase that prefers to use lactosyl lipids as acceptor substrates. PmST2 and PmST1 thus complement each other for an efficient synthesis of α2-3-linked sialosides with or without lipid portion. In addition, β1-4-linked galactosyl lipids are better PmST2 substrates than β1-3-linked galactosyl lipids. PmST2 has been used successfully in the preparative scale synthesis of sialyllactosyl sphingosine (lyso-GM3), which is an important glycolipid and an intermediate for synthesizing more complex glycolipids such as gangliosides.

Original languageEnglish (US)
Pages (from-to)1206-1216
Number of pages11
JournalGlycobiology
Volume21
Issue number9
DOIs
StatePublished - Sep 2011

Keywords

  • Glycolipid
  • lactosyl sphingosine
  • lyso-GM3
  • sialyllactosyl sphingosine
  • sialyltransferase

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'PmST2: A novel Pasteurella multocida glycolipid α2-3- sialyltransferase'. Together they form a unique fingerprint.

  • Cite this