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Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.

ABSTRACT: BACKGROUND: In a recent report, the carbohydrate-binding specificities of the plant lectins Galanthus nivalis (GNA) and the closely related lectin from Zea mays (GNAmaize) were determined by glycan array analysis and indicated that GNAmaize recognizes complex-type N-glycans whereas GNA has specificity towards high-mannose-type glycans. Both lectins are tetrameric proteins sharing 64% sequence similarity. RESULTS: GNAmaize appeared to be ~20- to 100-fold less inhibitory than GNA against HIV infection, syncytia formation between persistently HIV-1-infected HuT-78 cells and uninfected CD4+ T-lymphocyte SupT1 cells, HIV-1 capture by DC-SIGN and subsequent transmission of DC-SIGN-captured virions to uninfected CD4+ T-lymphocyte cells. In contrast to GNA, which preferentially selects for virus strains with deleted high-mannose-type glycans on gp120, prolonged exposure of HIV-1 to dose-escalating concentrations of GNAmaize selected for mutant virus strains in which one complex-type glycan of gp120 was deleted. Surface Plasmon Resonance (SPR) analysis revealed that GNA and GNAmaize interact with HIV IIIB gp120 with affinity constants (KD) of 0.33 nM and 34 nM, respectively. Whereas immobilized GNA specifically binds mannose oligomers, GNAmaize selectively binds complex-type GlcNAc?1,2Man oligomers. Also, epitope mapping experiments revealed that GNA and the mannose-specific mAb 2G12 can independently bind from GNAmaize to gp120, whereas GNAmaize cannot efficiently bind to gp120 that contained prebound PHA-E (GlcNAc?1,2man specific) or SNA (NeuAc?2,6X specific). CONCLUSION: The markedly reduced anti-HIV activity of GNAmaize compared to GNA can be explained by the profound shift in glycan recognition and the disappearance of carbohydrate-binding sites in GNAmaize that have high affinity for mannose oligomers. These findings underscore the need for mannose oligomer recognition of therapeutics to be endowed with anti-HIV activity and that mannose, but not complex-type glycan binding of chemotherapeutics to gp120, may result in a pronounced neutralizing activity against the virus.

SUBMITTER: Hoorelbeke B

PROVIDER: S-EPMC3048538 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.

Hoorelbeke Bart B Van Damme Els Jm EJ Rougé Pierre P Schols Dominique D Van Laethem Kristel K Fouquaert Elke E Balzarini Jan J

Retrovirology 20110211 1

<h4>Background</h4>In a recent report, the carbohydrate-binding specificities of the plant lectins Galanthus nivalis (GNA) and the closely related lectin from Zea mays (GNAmaize) were determined by glycan array analysis and indicated that GNAmaize recognizes complex-type N-glycans whereas GNA has specificity towards high-mannose-type glycans. Both lectins are tetrameric proteins sharing 64% sequence similarity.<h4>Results</h4>GNAmaize appeared to be ~20- to 100-fold less inhibitory than GNA agai ...[more]

PMID: 21314946

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Project description:BackgroundHealth risks arising from heavy metal pollution have attracted global attention. As a result, many studies on the accumulation of heavy metals in soil-plant systems have performed human health risk assessments.ObjectivesWe aimed to examine the ability of Zea mays (maize) to accumulate heavy metals and assess the bioaccumulation factor (BAF) by collecting, collating, and analyzing data on heavy metal concentrations in Zea mays.MethodsThis study reviewed the accumulation of five selected heavy metals, cadmium (Cd), chromium (Cr), lead (Pb), copper (Cu), and zinc (Zn) in soil and the corresponding BAF of Zea mays grown on those soils using a systematic search of peer-reviewed scientific journals. A total of 27 research works were reviewed after screening 52 articles for subject matter relevancy, including dumpsites, industrially polluted soils, inorganically fertilized soils, mining sites, smelting sites, municipal wastewater irrigated soils, and a battery waste dumpsite.ResultsAmong the reviewed sites, concentrations of Cd and Cr were highest at a tin mining site, where prolonged mining, mineral processing and other production activities contributed heavy metal pollution in the soil. The soil at a battery waste dumpsite exhibited the highest Pb concentration, while the soil at a Zn smelting site presented the highest concentration of Zn. The highest soil Cu concentration was found in an area where sewage irrigation had been carried out over a long period. The BAF of the five heavy metals in Zea mays increased with the metal concentrations in the soil. The BAF of Cd, Cr, Pb, Cu, and Zn in Zea mays from the study areas fall within the ranges of 0-0.95, 0-1.89, 0-1.20, 0.011-0.99, and 0.03-0.99, respectively. Cadmium and Zn had the highest bioconcentration factors values in maize plants, likely due to their higher mobility rate compared to the other heavy metals.ConclusionsThe study concluded that Zea mays is capable of accumulating high amounts of heavy metals, although accumulation of these heavy metals is influenced by multiple factors including soil texture, cation exchange capacity, root exudation and especially soil pH and chemical forms of the heavy metals. Zea mays should not be planted on metal-contaminated soils because of its potential to act as a hyperaccumulator.Competing interestsThe authors declare no competing financial interests.

Dataset Information

Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.

Publications

Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.

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