Identification of glycoproteins associated with HIV latently infected cells using quantitative glycoproteomics

Weiming Yang, Brooks Jackson, Hui Zhang

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

HIV infection is not curable due to viral latency. Compelling reports suggest that there is a distinct profile of surface proteins that can be used for targeting latently infected cells. We have recently reported that glycoproteins were differentially secreted from HIV latently infected ACH-2 cells compared to the parental A3.01 cells. This finding suggests that glyco-phenotype might be different in these two cell lines. To determine the difference, the ACH-2 and A3.01 cell lines were subjected to a glycoproteomic analysis. A total number of 940 unique N-linked glycosite-containing peptides from 515 glycoproteins were identified. Among the glycoproteins, 365 and 104 were annotated as cell surface and membrane-associated proteins, respectively. Quantitative LC-MS/MS analysis revealed a change of 236 glycosite-containing peptides from 172 glycoproteins between the two cell lines without reactivation. Bioinformatic analysis suggests that cell adhesion, immune response, glycoprotein metabolic process, cell motion, and cell activation were associated with the changed proteins. After reactivation of latency, changes in glycosite-containing peptides were observed in both cell lines. The changed proteins suggest that cell migration, response to wounding and immune response might be impaired in reactivated latently infected cells. Glycoproteomics merits future application using primary cells to discover reveal mechanisms in HIV pathogenesis.

Original languageEnglish (US)
Pages (from-to)1872-1880
Number of pages9
JournalProteomics
Volume16
Issue number13
DOIs
StatePublished - Jul 1 2016

Fingerprint

Glycoproteins
HIV
Cells
Peptides
Cell Line
Membrane Proteins
Cell adhesion
Bioinformatics
Virus Latency
Proteins
Chemical activation
Computational Biology
Cell Adhesion
HIV Infections
Cell Movement
Cell Membrane
Phenotype

Keywords

  • Glycoproteins
  • Glycoproteomics
  • HIV
  • Label-free quantitation
  • Latency

Cite this

Identification of glycoproteins associated with HIV latently infected cells using quantitative glycoproteomics. / Yang, Weiming; Jackson, Brooks; Zhang, Hui.

In: Proteomics, Vol. 16, No. 13, 01.07.2016, p. 1872-1880.

Research output: Contribution to journalArticle

Yang, Weiming ; Jackson, Brooks ; Zhang, Hui. / Identification of glycoproteins associated with HIV latently infected cells using quantitative glycoproteomics. In: Proteomics. 2016 ; Vol. 16, No. 13. pp. 1872-1880.
@article{685429aa703245bbb81c8e72ab80f72d,
title = "Identification of glycoproteins associated with HIV latently infected cells using quantitative glycoproteomics",
abstract = "HIV infection is not curable due to viral latency. Compelling reports suggest that there is a distinct profile of surface proteins that can be used for targeting latently infected cells. We have recently reported that glycoproteins were differentially secreted from HIV latently infected ACH-2 cells compared to the parental A3.01 cells. This finding suggests that glyco-phenotype might be different in these two cell lines. To determine the difference, the ACH-2 and A3.01 cell lines were subjected to a glycoproteomic analysis. A total number of 940 unique N-linked glycosite-containing peptides from 515 glycoproteins were identified. Among the glycoproteins, 365 and 104 were annotated as cell surface and membrane-associated proteins, respectively. Quantitative LC-MS/MS analysis revealed a change of 236 glycosite-containing peptides from 172 glycoproteins between the two cell lines without reactivation. Bioinformatic analysis suggests that cell adhesion, immune response, glycoprotein metabolic process, cell motion, and cell activation were associated with the changed proteins. After reactivation of latency, changes in glycosite-containing peptides were observed in both cell lines. The changed proteins suggest that cell migration, response to wounding and immune response might be impaired in reactivated latently infected cells. Glycoproteomics merits future application using primary cells to discover reveal mechanisms in HIV pathogenesis.",
keywords = "Glycoproteins, Glycoproteomics, HIV, Label-free quantitation, Latency",
author = "Weiming Yang and Brooks Jackson and Hui Zhang",
year = "2016",
month = "7",
day = "1",
doi = "10.1002/pmic.201500215",
language = "English (US)",
volume = "16",
pages = "1872--1880",
journal = "Proteomics",
issn = "1615-9853",
publisher = "Wiley-VCH Verlag",
number = "13",

}

TY - JOUR

T1 - Identification of glycoproteins associated with HIV latently infected cells using quantitative glycoproteomics

AU - Yang, Weiming

AU - Jackson, Brooks

AU - Zhang, Hui

PY - 2016/7/1

Y1 - 2016/7/1

N2 - HIV infection is not curable due to viral latency. Compelling reports suggest that there is a distinct profile of surface proteins that can be used for targeting latently infected cells. We have recently reported that glycoproteins were differentially secreted from HIV latently infected ACH-2 cells compared to the parental A3.01 cells. This finding suggests that glyco-phenotype might be different in these two cell lines. To determine the difference, the ACH-2 and A3.01 cell lines were subjected to a glycoproteomic analysis. A total number of 940 unique N-linked glycosite-containing peptides from 515 glycoproteins were identified. Among the glycoproteins, 365 and 104 were annotated as cell surface and membrane-associated proteins, respectively. Quantitative LC-MS/MS analysis revealed a change of 236 glycosite-containing peptides from 172 glycoproteins between the two cell lines without reactivation. Bioinformatic analysis suggests that cell adhesion, immune response, glycoprotein metabolic process, cell motion, and cell activation were associated with the changed proteins. After reactivation of latency, changes in glycosite-containing peptides were observed in both cell lines. The changed proteins suggest that cell migration, response to wounding and immune response might be impaired in reactivated latently infected cells. Glycoproteomics merits future application using primary cells to discover reveal mechanisms in HIV pathogenesis.

AB - HIV infection is not curable due to viral latency. Compelling reports suggest that there is a distinct profile of surface proteins that can be used for targeting latently infected cells. We have recently reported that glycoproteins were differentially secreted from HIV latently infected ACH-2 cells compared to the parental A3.01 cells. This finding suggests that glyco-phenotype might be different in these two cell lines. To determine the difference, the ACH-2 and A3.01 cell lines were subjected to a glycoproteomic analysis. A total number of 940 unique N-linked glycosite-containing peptides from 515 glycoproteins were identified. Among the glycoproteins, 365 and 104 were annotated as cell surface and membrane-associated proteins, respectively. Quantitative LC-MS/MS analysis revealed a change of 236 glycosite-containing peptides from 172 glycoproteins between the two cell lines without reactivation. Bioinformatic analysis suggests that cell adhesion, immune response, glycoprotein metabolic process, cell motion, and cell activation were associated with the changed proteins. After reactivation of latency, changes in glycosite-containing peptides were observed in both cell lines. The changed proteins suggest that cell migration, response to wounding and immune response might be impaired in reactivated latently infected cells. Glycoproteomics merits future application using primary cells to discover reveal mechanisms in HIV pathogenesis.

KW - Glycoproteins

KW - Glycoproteomics

KW - HIV

KW - Label-free quantitation

KW - Latency

UR - http://www.scopus.com/inward/record.url?scp=84990251635&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84990251635&partnerID=8YFLogxK

U2 - 10.1002/pmic.201500215

DO - 10.1002/pmic.201500215

M3 - Article

C2 - 27195445

AN - SCOPUS:84990251635

VL - 16

SP - 1872

EP - 1880

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 13

ER -