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PmST2: a novel Pasteurella multocida glycolipid α2-3-sialyltransferase
1Department of Chemistry, University of California, Davis, CA 95616, USA.
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.
Insights
Pasteurella multocida sialyltransferases PmST1 and PmST2 synthesize α2-3-linked sialosides. PmST2 is a novel glycolipid sialyltransferase crucial for synthesizing important glycolipids like lyso-GM3.
Area of Science:
- Microbiology
- Glycobiology
- Biochemistry
Background:
- Pasteurella multocida (Pm) is a significant pathogen affecting animals and humans.
- Sialylation plays a critical role in Pm pathogenesis.
- Three putative sialyltransferase genes exist in Pm strain Pm70.
Purpose of the Study:
- To characterize the novel glycolipid α2-3-sialyltransferase (PmST2) from Pm strain P-1059.
- To understand the complementary roles of PmST1 and PmST2 in sialoside synthesis.
- To explore the application of PmST2 in synthesizing complex glycolipids.
Main Methods:
- Enzymatic characterization of PmST2 using various acceptor substrates.
- Comparative analysis of PmST1 and PmST2 activity.
- Preparative scale synthesis of sialyllactosyl sphingosine (lyso-GM3) using PmST2.
Main Results:
- PmST2 is a novel glycolipid α2-3-sialyltransferase with a preference for lactosyl lipids.
- PmST1 and PmST2 exhibit complementary activities for efficient sialoside synthesis.
- PmST2 efficiently synthesizes lyso-GM3, a key intermediate for ganglioside synthesis.
- β1-4-linked galactosyl lipids are preferred PmST2 substrates over β1-3-linked ones.
Conclusions:
- PmST2 is a unique glycolipid sialyltransferase that complements PmST1.
- The combined action of PmST1 and PmST2 facilitates diverse sialoside synthesis in Pm.
- PmST2 holds potential for the preparative synthesis of important glycolipids.
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