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Precision mapping of glycosite-specific glycans reveals distinctive N-glycosylation on human spermatozoa

ABSTRACT: In this study, we applied the recently developed software, StrucGP to large-scale characterize glycoproteins, and IGPs, as well as precise site-specific glycan structures in human spermatozoa. Furthermore, bioinformatical analyses were conducted to systematically describe the potential functions of N-glycosylation in human spermatozoa.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Testis, Sperm

DISEASE(S): Disease Free

SUBMITTER: Miaomiao Xin

LAB HEAD: Shisheng Sun

PROVIDER: PXD026649 | Pride | 2022-05-19

REPOSITORIES: Pride

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Precision Glycoproteomics Reveals Distinctive N-Glycosylation in Human Spermatozoa.

Xin Miaomiao M You Shanshan S Xu Yintai Y Shi Wenhao W Zhu Bojing B Shen Jiechen J Wu Jingyu J Li Cheng C Chen Zexuan Z Su Yuanjie Y Shi Juanzi J Sun Shisheng S

Molecular & cellular proteomics : MCP 20220218 4

Spermatozoon represents a very special cell type in human body, and glycosylation plays essential roles in its whole life including spermatogenesis, maturation, capacitation, sperm-egg recognition, and fertilization. In this study, by mapping the most comprehensive N-glycoproteome of human spermatozoa using our recently developed site-specific glycoproteomic approaches, we show that spermatozoa contain a number of distinctive glycoproteins, which are mainly involved in spermatogenesis, acrosome ...[more]

PMID: 35183770

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