While structural information on biomolecules is mainly obtained from purified in vitro samples, NMR can also be applied in the context of entire cells or organisms. The present study describes maturation processes in living Salmonella enterica serovar Typhimurium, a prevalent cause for human gastroenteritis. In our physiological study, we follow the composition of the O-antigen on the outer bacterial membrane with high-resolution MAS NMR spectroscopy. We detect and characterize an evolution of the O-antigen composition, in particular of the O-acetylation state of the O-antigen, a factor that can play an important role in vaccine development.

O-antigen, O-acetylation, Salmonella enterica, outer membrane, Typhimurium, MAS NMR spectroscopy

13C NMR data:
missing...
1H NMR data:
Linkage	Residue	H1	H2	H3	H4	H5	H6
3,4,3,2	Ac	-	2.09
3,4,3	aXAbep	5.25	5.06	2.06	3.93	4.15	1.20
3,4	aDManp	5.37	3.96	3.95	?	?	?
3	aLRhap	5.04	4.07	3.97	3.55	3.92	1.33
4	aDGlcp
	aDGalp	5.15	3.91	?	4.06	4.12	3.72

There is only one chemically distinct structure:

SVGMWSMILES3D molIonize

 

*O[C@H]1[C@@H](O[C@H]2O[C@H](C)[C@H](O)C[C@H]2OC(C)=O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@H]1[C@H](C)O[C@@H](O[C@@H]2[C@@H](O)[C@@H](*)O[C@H](CO)[C@@H]2O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H]1O

804.745 g/mol (C₃₂H₅₂R₂O₂₃, R = next and previous repeats, not counted in mol weight)