Journal article
Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma
Clinical proteomics, Vol.11(1), pp.9-9
2014
DOI: 10.1186/1559-0275-11-9
PMCID: PMC4015807
PMID: 24597896
Abstract
Glycoproteins secreted into plasma from T cells infected with human immunodeficiency virus (HIV) latent infection may provide insight into understanding the host response to HIV infection
in vivo
. Glycoproteomics, which evaluates the level of the glycoproteome, remains a novel approach to study this host response to HIV. In order to identify human glycoproteins secreted from T cells with latent HIV infection, the medium from cultured HIV replication-competent T cells was compared with the medium from cultured parental A3.01 cells via solid phase extraction of glycopeptides (SPEG) and high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). Using these methods, 59 human glycoproteins were identified as having significantly different abundance levels between the media from these two cell lines. The relevance of these 59 proteins to HIV infection
in vivo
was assessed in plasma from HIV
+
and HIV
-
subjects. Comparison between T cell and plasma revealed that six glycoproteins (galectin-3-binding protein, L-selectin, neogenin, adenosine deaminase CECR1, ICOS ligand and phospholipid transfer protein) were significantly elevated in the HIV
+
T cells and plasma studies. These findings suggest that the response of T cells harboring latent HIV infection contributed, in part, to the glycoprotein changes in HIV
+
plasma. These proteins, once validated, could provide insight into host-HIV interaction.
Details
- Title: Subtitle
- Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma
- Creators
- Weiming Yang - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USAJian-Ying Zhou - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USALi Chen - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USAMinghui Ao - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USAShisheng Sun - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USAPaul Aiyetan - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USAAntoine Simmons - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USAHui Zhang - Johns Hopkins UniversityJay Brooks Jackson - Department of Pathology, Johns Hopkins University School of Medicine, 1550 Orleans Street, CRBII, Room 3 M-03, Baltimore MD 21205, USA
- Resource Type
- Journal article
- Publication Details
- Clinical proteomics, Vol.11(1), pp.9-9
- DOI
- 10.1186/1559-0275-11-9
- PMID
- 24597896
- PMCID
- PMC4015807
- NLM abbreviation
- Clin Proteomics
- ISSN
- 1542-6416
- eISSN
- 1559-0275
- Publisher
- Springer
- Language
- English
- Date published
- 2014
- Academic Unit
- Pathology; VPMA - Administration
- Record Identifier
- 9984047649102771
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