Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Glycan_and_spectra.rar	Other
	Sperm_cotton_fraction10_IGP1_Xin_20210208.raw	Raw
	Sperm_cotton_fraction10_IGP1_Xin_20210208_result.xlsx	Xlsx
	Sperm_cotton_fraction10_IGP2_Xin_20210208.raw	Raw
	Sperm_cotton_fraction10_IGP2_Xin_20210208_result.xlsx	Xlsx

Items per page:

1 - 5 of 75

Publications

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

Similar Datasets

Profiling of human spermatozoa glycoproteins by LC/MS/MS

Project description:N-linked glycoproteins are known to be important for spermatozoa development and gametes fusion. However, little is known about detailed information of these glycoproteins, particularly the glycosylation sites and its corresponding glycan structures in human spermatozoa. In present study, an in house software coupled with LC-MS/MS analysis of intact glycopeptides was employed to establish a large scale of site-specific N-glycoproteome map in human spermatozoa. The results mapped the large-scale N-glycoproteins in human spermatozoa and interpreted the precise glycan structures with the corresponding glycosites. These presented data laid the foundation for the exploration of biological function of glycosylation on human spermatozoa and glycan structure involved male infertility.

2023-03-04 | PXD020286 | Pride

Structural- and Site-specific N-glycosylation Characterization of COVID-19 Virus Spike with StrucGP

Project description:Spike (S) protein plays a key role in COVID-19 (SARS-CoV-2) infection and host-cell entry. Previous studies have systematically analyzed site-specific glycans compositions of S protein. Here, we further provide structure-clear N-glycosylation of S protein at site-specific level by using our recently developed structure- and site-specific N-glycoproteomics sequencing algorithm StrucGP. In addition to the common N-glycans as detected in previous studies, many uncommon glycosylation structures such as LacdiNAc structures, Lewis structures, Mannose 6-Phosphate (M6P) residues and bisected core structures were unambiguously mapped at a total of 20 glycosites in the S protein trimer and protomer. These data further supports the glycosylation structural-functional investigations of COVID-19 virus Spike.

2022-10-13 | PXD034086 | Pride

Structural Interpretation of Glycosite-specific N-Glycans Using Tandem Mass Spectrometry

Project description:In this project we developed a new algorithm termed StrucGP, for large-scale interpretation of N-glycan structures on intact glycopeptides from tandem mass spectrometry data. StrucGP is able to reveal the glycan structure heterogeneity for individual glycosites. The StrucGP also has high performance in distinguishing various structure isoforms and identifying new and rare glycan structures from complex samples.

2021-07-07 | PXD025859 | Pride

Precision structural interpretation of site-specific N-glycans in seminal plasma

Project description:This study is aimed to comprehensively and globally characterize seminal plasma glycoproteins in a site-specific manner with information of N-glycosites and corresponding glycan structures, as well as glycan isomers using mass spectrometry. Furthermore, the function of specific glycan structures is introduced during human reproduction. In addition, site-specific glycoproteins are compared precisely to explored the sub-glycan structure regulation of glycoprotein in human seminal plasma and spermatozoa.

2023-03-04 | PXD030804 | Pride

Glycoproteomics of human THP-1-derived M0, M1 and M2 macrophages

Project description:In this study, we used human THP-1-derived macrophages as an immune cell model, and systematically performed glycoproteomics of three subtypes of macrophages by StrucGP.To study the N‑Glycoproteomic of them, the intact glycopeptides were first enriched and identified using triplicate mass spectrometry (MS)-based glycoproteomic approaches, then StrucGP was used for subsequent analysis. In total three subtypes of macrophages, these intact glycopeptides consist of 253 N-linked glycan structures at 652 unique glycosites from 372 N-glycoproteins, along with their PSM information. A total of 135, 163, and 201 N-glycan structures were identified from M0, M1, and M2 macrophages, respectively.

2023-10-19 | PXD030277 | Pride

N-glycoproteimics of human serum proteins

Project description:In this study, precision N-glycan structure characterization of human serum was established at site-specific level by using our recently developed glycan structure interpretation software, StrucGP.

2024-04-22 | PXD048751 | Pride

Precision Characterization of Site-specific O-Acetylated Sialic Acids on N-Glycoproteins

Project description:O-Acetylation is a common modification of sialic acid, playing a significant role in glycoprotein stability, immune response, and cell development. The lack of efficient methods for direct analysis of O-acetylated sialoglycopeptides (O-AcSGPs) made the majority of identified O-acetylated sialic acids (O-AcSia) till now had no glycosite/glycoprotein information. Herein, we introduced a new workflow for precise interpretation of O-AcSGPs with probability estimation by recognizing the characteristic B and Y ions of O-AcSias.

2023-01-13 | PXD037161 | Pride

Evaluation of absorbent cotton for glycopeptide enrichment

Project description:This study introduced the use of cotton in 200µL tips, namely cotton HILIC as a convenient tool for enriching large-scale glycopeptides before MS analysis in this study. The optimal loading buffer for cotton HILIC was investigated by using mouse brain as a complex test sample. Subsequently, the performance of cotton HILIC was evaluated by comparing with other two commercial enrichment approaches, venusil HILIC and Oasis MAX in both mouse brain and seminal plasma. Moreover, capacity and recovery rate were evaluated using different milligram of cotton in 200µL tips. Thus, a simple, convenient, and cost-friendly cotton HILIC method was proposed to achieve highly selective intact glycopeptide profiling.

2023-03-04 | PXD035078 | Pride

Expression data from pig oviduct in response to X or Y chromosome bearing spermatozoa

Project description:The objective of the present study is to investigate if females have the ability to recognise X or Y chromosome bearing spermatozoa and present a different response to different spermatozoa. In order to investigate if females have the ability to recognise X or Y chromosome bearing spermatozoa and present a different response to different spermatozoa. Samples of semen were sorted for chromosomal sex by M-oM-,M-^Bow cytometric-sorting. Using laparoscopic insemination one oviduct was inseminated with X spermatozoa and the contralateral oviduct was inseminated with Y spermatozoa.This allowed us to obtain samples from the oviduct in contact with X sperm and Y sperm in the the contrlateral oviduct from the same sow. Oviduct pig samples were collected for RNA isolation and hybridization on Affymetrix microarrays. Four biological replicates were performed (n= 4 sows) and a total of 8 arrays were used for microarrays study (4 arrays for oviduct samples in contact with X spermatozoa and 4 arrays for oviduct samples in contact with Y spermatozoa.

2014-05-20 | E-GEOD-47139 | biostudies-arrayexpress

Repressive and active histone methylation mark distinct promoters in human and mouse spermatozoa

Project description:This SuperSeries is composed of the following subset Series: GSE13863: Repressive and active histone methylation mark distinct promoters in human and mouse spermatozoa (Nimblegen) GSE19889: Repressive and active histone methylation mark distinct promoters in human and mouse spermatozoa (Illumina) Refer to individual Series

2010-05-16 | E-GEOD-19892 | biostudies-arrayexpress