A quantitative method for analyzing glycome profiles of plant cell walls
Journal Article
·
· Carbohydrate Research
- University of Georgia, Athens, GA (United States); DOE/OSTI
- University of Georgia, Athens, GA (United States)
- University of Georgia, Athens, GA (United States); University of Georgia, Aiken, SC (United States). Savannah River Ecology Laboratory
Glycome profiling allows for the characterization of plant cell wall ultrastructure via sequential extractions and subsequent detection of specific epitopes with a suite of glycan-specific monoclonal antibodies (mAbs). The data are often viewed as the amount of materials recovered and coinciding colored heatmaps of mAb binding are generated. Interpretation of these data can be considered qualitative in nature as it depends on detecting subtle visual differences in antibody binding strength. In this paper we report a mixed model-based quantitative approach for glycome profile analyses, which accounts for the amount of materials recovered and displays the normalized values in revised heatmaps and statistical heatmaps depicting significant differences. The utility of this methodology was demonstrated on a previously published dataset investigating the effects of moisture stress on the roots and needles of Pinus taeda. An annotated R script for the quantitative methodology is included to allow future studies to utilize the same approach.
- Research Organization:
- University of Georgia, Athens, GA (United States)
- Sponsoring Organization:
- Agriculture and Food Research Initiative; National Institute of Food and Agriculture; National Science Foundation (NSF); USDOE; USDOE Office of Environmental Management (EM)
- Grant/Contract Number:
- EM0004391
- OSTI ID:
- 1533601
- Alternate ID(s):
- OSTI ID: 1547088
- Journal Information:
- Carbohydrate Research, Journal Name: Carbohydrate Research Journal Issue: C Vol. 448; ISSN 0008-6215
- Publisher:
- ElsevierCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Similar Records
Improving neutralization potency and breadth by combining broadly reactive HIV-1 antibodies targeting major neutralization epitopes
Journal Article
·
Wed Feb 04 23:00:00 EST 2015
· Journal of Virology
·
OSTI ID:1352359