Glycan specificity of neuraminidases determined in microarray format

Janet E. McCombs, Jason P. Diaz, Kevin J. Luebke, Jennifer J. Kohler

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Neuraminidases hydrolytically remove sialic acids from glycoconjugates. Neuraminidases are produced by both humans and their pathogens, and function in normal physiology and in pathological events. Identification of neuraminidase substrates is needed to reveal their mechanism of action, but high-throughput methods to determine glycan specificity of neuraminidases are limited. Here we use two glycan labeling reactions to monitor neuraminidase activity toward glycan substrates. While both periodate oxidation and aniline-catalyzed oxime ligation (PAL) and galactose oxidase and aniline-catalyzed oxime ligation (GAL) can be used to monitor neuraminidase activity toward glycans in microtiter plates, only GAL accurately measured neuraminidase activity toward glycans displayed on a commercial glass slide microarray. Using GAL, we confirm known linkage specificities of three pneumococcal neuraminidases and obtain new information about underlying glycan specificity.

Original languageEnglish (US)
Pages (from-to)31-40
Number of pages10
JournalCarbohydrate Research
StatePublished - Jun 16 2016


  • Chemoenzymatic labeling
  • Microarray
  • Neuraminidase
  • Sialic acids

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry


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