Unique gangliosides synthesized in vitro by sialyltransferases from marine bacteria and their characterization: ganglioside synthesis by bacterial sialyltransferases.
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ABSTRACT: On the basis of the results outlined in our previous report, bacterial sialyltransferases (ST) from marine sources were further characterized using glycosphingolipids (GSL), especially ganglio-series GSLs, based on the enzymatic characteristics and kinetic parameters obtained by Line weaver-Burk plots. Among them, GA1 and GA2 were found to be good substrates for these unique STs. Thus, new gangliosides synthesized by ?2-3 and ?2-6STs were structurally characterized by several analytical procedures. The ganglioside generated by the catalytic activity of ?2-3ST was identified as GM1b. On the other hand, when enzyme reactions by ?2-6STs were performed using substrates GA2 and GA1, very unique gangliosides were generated. The structures were identified as NeuAc?2-6GalNAc?1-4Gal?1-4Glc?-Cer and NeuAc?2-6Gal?1-3GalNAc?1-4Gal?1-4Glc?-Cer, respectively. The synthesized ganglioside NeuAc?2-6GalNAc?1-4Gal?1-4Glc?-Cer showed binding activity to the influenza A virus {A/Panama/2007/99 (H3N2)} at a similar level to purified sialyl(?2-3)paragloboside (S2-3PG) and sialyl(?2-6)paragloboside (S2-6PG) from mammalian sources. The evidence suggests that these STs have unique features, including substrate specificities restricted not only to lacto-series but also to ganglio-series GSLs, as well as catalytic potentials for ganglioside synthesis. This evidence demonstrates that effective in vitro ganglioside synthesis could be a valuable tool for selectively synthesizing sialic acid (Sia) modifications, thereby preparing large-scale gangliosides and permitting the exploration of unknown functions.
SUBMITTER: Kamimiya H
PROVIDER: S-EPMC3617933 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
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