Determination of the binding affinities of Neisseria meningitidis serogroup W capsule polymerase with two nucleotide sugar substrates

BMC Research Notes
Abeer SharyanPumtiwitt C McCarthy

Abstract

Meningococcal meningitis is a public health burden. Immunization strategies have reduced global incidence of the disease. Glycoconjugate vaccines are the most effective type of vaccine to combat most causes of meningococcal meningitis. These vaccines contain capsular polysaccharide fragments from disease-causing serogroups of Neisseria meningitidis that are chemically attached to a carrier protein. The enzymes responsible for capsular polysaccharide synthesis can serve as tools to make these critical vaccine components. One such enzyme is the N. meningitidis serogroup W capsule polymerase. This enzyme is responsible for creating the galactose-sialic acid containing capsular polysaccharide of this serogroup. Our aim in this study was to determine the binding affinities of nucleotide sugar donors CMP-sialic acid and UDP-galactose using a coupled transferase assay to inform future work to modulate polysaccharide synthesis by this enzyme. We determined a Km of 66.8 µM for CMP-sialic acid and a Km for UDP-galactose of 3.9 µM. These values are lower than reported values for other retaining galactosyltransferases and inverting sialyltransferases respectively. There were difficulties obtaining reliable data for galactosyltransferase ac...Continue Reading

References

Jul 1, 1994·Analytical Biochemistry·S GosselinM M Palcic
Jan 20, 2007·FEMS Microbiology Reviews·David S Stephens
Nov 26, 2010·Glycobiology·Magali AudryChristelle Breton
Feb 1, 2011·Journal of Bacteriology·Dwight C PetersonWillie F Vann
Mar 3, 2018·Vaccines·Pumtiwitt C McCarthyLaleh Sheikhi Moghaddam

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Methods Mentioned

BETA
transferase assay

Software Mentioned

GraphPad Prism

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