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Synthesis of biologically active N- and O-linked glycans with multisialylated poly-N-acetyllactosamine extensions using P. damsela α2-6 sialyltransferase

Academic Article
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Overview

related to degree

  • Polonskaya, Zinaida M, Ph.D. in Biology, Scripps Research 2008 - 2014

authors

  • Nycholat, C. M.
  • Peng, W.
  • McBride, R.
  • Antonopoulos, A.
  • de Vries, R. P.
  • Polonskaya, Zinaida M
  • Finn, M.G.
  • Dell, A.
  • Haslam, S. M.
  • Paulson, James

publication date

  • December 2013

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Sialosides on N- and O-linked glycoproteins play a fundamental role in many biological processes, and synthetic glycan probes have proven to be valuable tools for elucidating these functions. Though sialic acids are typically found α2-3- or α2-6-linked to a terminal nonreducing end galactose, poly-LacNAc extended core-3 O-linked glycans isolated from rat salivary glands and human colonic mucins have been reported to contain multiple internal Neu5Acα2-6Gal epitopes. Here, we have developed an efficient approach for the synthesis of a library of N- and O-linked glycans with multisialylated poly-LacNAc extensions, including naturally occurring multisialylated core-3 O-linked glycans. We have found that a recombinant α2-6 sialyltransferase from Photobacterium damsela (Pd2,6ST) exhibits unique regioselectivity and is able to sialylate internal galactose residues in poly-LacNAc extended glycans which was confirmed by MS/MS analysis. Using a glycan microarray displaying this library, we found that Neu5Acα2-6Gal specific influenza virus hemagglutinins, siglecs, and plant lectins are largely unaffected by adjacent internal sialylation, and in several cases the internal sialic acids are recognized as ligands. Polyclonal IgY antibodies specific for internal sialoside epitopes were elicited in inoculated chickens.

subject areas

  • Humans
  • Photobacterium
  • Polysaccharides
  • Sialic Acids
  • Sialyltransferases
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Identity

PubMed Central ID

  • PMC3901641

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja409781c

PubMed ID

  • 24256304
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Additional Document Info

start page

  • 18280

end page

  • 18283

volume

  • 135

issue

  • 49

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