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Structural and functional characterization of glycosyltransferases in the Campylobacter concisus N-linked glycoconjugate biosynthetic pathway

Award Number: F32GM146421
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: FELLOWSHIP/SCHOLARSHIP/STUDENT LOANS
PERIOD OF PERFORMANCE START DATE: 02/01/2023
PERIOD OF PERFORMANCE END DATE: 01/31/2025

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Structural and functional characterization of glycosyltransferases in the Campylobacter concisus N-linked glycoconjugate biosynthetic pathway - Bacterial glycoconjugates are a diverse group of macromolecules that play a key role in bacterial survival and pathogenicity by mediating bacteria-host interactions. Despite their structural diversity, many glycoconjugates are made by prokaryotes utilizing a common mechanism, which includes transferring glycans to a Pren-PP- linked carrier at the membrane interface. The striking diversity of glycoconjugates is achieved through sequential addition of glycans by glycosyltransferases (GTs), which transfer sugars from soluble nucleotide-activated donors (NDP-sugars) to the lipid-based carrier molecule. Despite being ubiquitous across all kingdoms of life, GTs still represent an excellent target for antibiotics, due to the remarkable degree of selectivity they exhibit for structurally very similar sugars. Understanding the structural features that influence GT substrate selectivity and protein-protein interactions in pathogenic bacteria like Campylobacter species is critical for antibiotic development, and this research proposal strives to address that knowledge gap. To date, the substrates for C. jejuni GTs have been confirmed in the Campylobacter genus, but structural information for PglA, PglJ, PglH1, and PglH2 of C. concisus, another clinically significant human pathogen, is still unavailable. Additionally, characterizing GTs from the same organism's glycoconjugate biosynthetic pathway will offer the structural information needed for future protein-protein interaction studies and will pave the way for analysis to clarify how these proteins interact to modulate pathway flux. Aim 1 of this proposal will identify preferred GT substrates using nano-differential scanning fluorimetry (nanoDSF) and determine steady-state kinetic parameters using luminescence-based GT activity assays. Aim 2 will be to discover the detergent and buffer conditions required for crystallization of purified GTs, as well as to optimize protein crystals and collect X-ray crystal data to obtain high-resolution crystal structures. Aim 3 will be to characterize a number of orthologs from a GT-B sequence similarity network (SSN) in order to gain insight into GT evolution and to pinpoint the primary sequence variables that account for their various substrate specificities. Interprotein covariance between GT residues will be investigated via the GREMLIN method in order to identify interactions responsible for the hypothesized formation of supramolecular complexes between these enzymes. The resulting findings will reveal binding determinants controlling specificity for glycans prevalent in pathogenic prokaryotes and demonstrate crucial structure-function links and protein-protein interactions.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2026 ( Subtotal = -$1,443 )
2026	2024	TRUSTEES OF BOSTON UNIVERSITY	1 SILBER WAY	BOSTON	MA	02215	SUFFOLK	USA	Biomedical Research and Research Training	000	2	1/27/2026	NON-COMPETING CONTINUATION	-$1,443
														Subtotal = -$1,443

Issue Date FY: 2024 ( Subtotal = $76,756 )
2024	2024	TRUSTEES OF BOSTON UNIVERSITY	1 SILBER WAY	BOSTON	MA	02215	SUFFOLK	USA	Biomedical Research and Research Training	001	2	5/13/2024	NON-COMPETING CONTINUATION	$4,964
2024	2024	TRUSTEES OF BOSTON UNIVERSITY	1 SILBER WAY	BOSTON	MA	02215	SUFFOLK	USA	Biomedical Research and Research Training	000	2	12/19/2023	NON-COMPETING CONTINUATION	$71,792
														Subtotal = $76,756

Issue Date FY: 2023 ( Subtotal = $69,500 )
2023	2023	TRUSTEES OF BOSTON UNIVERSITY	1 SILBER WAY	BOSTON	MA	02215	SUFFOLK	USA	Biomedical Research and Research Training	002	1	2/9/2023	NEW	$0
2023	2023	TRUSTEES OF BOSTON UNIVERSITY	1 SILBER WAY	BOSTON	MA	02215	SUFFOLK	USA	Biomedical Research and Research Training	000	1	1/18/2023	NEW	$67,582
2023	2023	TRUSTEES OF BOSTON UNIVERSITY	1 SILBER WAY	BOSTON	MA	02215	SUFFOLK	USA	Biomedical Research and Research Training	001	1	2/9/2023	NEW	$1,918
														Subtotal = $69,500

Grand Total All Awards = $144,813

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Structural and functional characterization of glycosyltransferases in the Campylobacter concisus N-linked glycoconjugate biosynthetic pathway

Award Number: F32GM146421

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: FELLOWSHIP/SCHOLARSHIP/STUDENT LOANS

PERIOD OF PERFORMANCE START DATE: 02/01/2023

PERIOD OF PERFORMANCE END DATE: 01/31/2025

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