Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468474 | PMC |
| http://dx.doi.org/10.1128/JVI.00230-15 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Unraveling -Glycan Diversity of Mucins: Insights from SmE Mucinase and Ultraviolet Photodissociation Mass Spectrometry.
Anal Chem
December 2024
Department of Chemistry, University of Texas, Austin, Texas 78712, United States.
Article Synopsis
- The study focuses on understanding the complex patterns of -glycosylation in mucin domain proteins, which are important in diseases like cancer.
- Researchers are developing new methods to analyze these glycoproteins due to the difficulties presented by their diverse glycosylation structures.
- They combine the use of a targeted protease and ultraviolet photodissociation mass spectrometry to identify and map glycoforms of proteins like TIM-1, MUC-1, and MUC-16, further revealing glycosylation trends in these proteins.
4-plex quantitative glycoproteomics using glycan/protein-stable isotope labeling in cell culture.
J Proteomics
January 2025
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, United States. Electronic address:
Alterations in glycoprotein abundance and glycan structures are closely linked to numerous diseases. The quantitative exploration of glycoproteomics is pivotal for biomarker discovery, but comprehensive analysis within biological samples remains challenging due to low abundance, complexity, and lack of universal technology. We developed a multiplex glycoproteomic approach using an LC-ESI-MS platform for direct comparison of glycoproteomic quantitation.
View Article and Find Full Text PDFFollicle-Stimulating Hormone Sweetness: How Carbohydrate Structures Impact on the Biological Function of the Hormone.
Arch Med Res
December 2024
Department of Biomedical Sciences, State University of New York at Albany, Albany, NY, USA.
Follicle-stimulating hormone (FSH), or follitropin, exists in multiple molecular forms due largely to its protein-carbohydrate composition and the complexity of the glycans attached to the protein core. The heterogeneity of gonadotropins exists in two forms, macroheterogeneity, which results from the absence of one or two oligosaccharide chains in the ß-subunit, and microheterogeneity which results from variation in the structures and complexity of the glycans attached to the hormone. In the clinical arena, FSH compounds are widely used by fertility specialists to promote ovarian follicle growth and maturation to a preovulatory follicle containing a fertilization-competent oocyte.
View Article and Find Full Text PDFHydrophilic Interaction Chromatography Coupled to Ultraviolet Photodissociation Affords Identification, Localization, and Relative Quantitation of Glycans on Intact Glycoproteins.
J Proteome Res
October 2024
Department of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.
Protein glycosylation is implicated in a wide array of diseases, yet glycoprotein analysis remains elusive owing to the extreme heterogeneity of glycans, including microheterogeneity of some of the glycosites (amino acid residues). Various mass spectrometry (MS) strategies have proven tremendously successful for localizing and identifying glycans, typically utilizing a bottom-up workflow in which glycoproteins are digested to create glycopeptides to facilitate analysis. An emerging alternative is top-down MS that aims to characterize intact glycoproteins to allow precise identification and localization of glycans.
View Article and Find Full Text PDFExpanding the structural resolution of glycosylation microheterogeneity in therapeutic proteins by salt-free hydrophilic interaction liquid chromatography tandem mass spectrometry.
MAbs
August 2024
Protein Analytical Chemistry, Genentech, A Member of the Roche Group, South San Francisco, CA, USA.
Article Synopsis
- * Traditional methods for analyzing glycans often fall short in either structural detail or specificity, with the commonly used techniques having their own limitations regarding salt content and sensitivity.
- * This research presents a new method, salt-free glycopeptide-based HILIC-MS/MS, which allows for simultaneous identification, separation of glycan isomers, and site-specific information, enhancing the analysis of important quality attributes in biopharmaceuticals.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!