Abstract O-acetylation is a common modification of sialic acids that has been implicated in a multitude of biological and disease processes.A lack of analytical methods that can determine exact structures of sialic acid variants is a hurdle to determine roles of distinct O-acetylated sialosides.Here, we describe a drift tube ion mobility-mass spectrometry approach that can elucidate exact O-acetylation patterns as well as glycosidic linkage types of kt196 torque converter sialosides isolated from complex biological samples.It is based on the use of a library of synthetic O-acetylated read more sialosides to establish intrinsic collision cross section (CCS) values of diagnostic fragment ions.
The CCS values were used to characterize O-acetylated sialosides from mucins and N-linked glycans from biologicals as well as equine tracheal and nasal tissues.It uncovered contrasting sialic acid linkage types of acetylated and non-acetylated sialic acids and provided a rationale for sialic acid binding preferences of equine H7 influenza A viruses.