Structure-Function Relations of Carbohydrates by Neoglycolipid Arrays

Huang, Gangliang; Huang, Hualiang; Zhang, Hou-Cheng; Wang, Peng-George

doi:10.1385/abab:133:3:211

Cited by 4 publications

(2 citation statements)

References 9 publications

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“…Non-catalytic domains of these proteins bind reversibly to specific monosaccharides or complex glycans to carry out biological functions [69]. The physiological roles of plant lectins are widely debated, ranging from growth regulation [70], plant development [71], seed storage [72] and defense against pest and pathogens [73,74]. The role of lectins in plant defense against insect herbivory is of great interest and a broad spectrum of plant lectins has been tested for insecticidal activity.…”

Section: Plant Defense Proteins: Lectinsmentioning

confidence: 99%

Toxins for Transgenic Resistance to Hemipteran Pests

Chougule

Bonning

2012

Toxins

139

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The sap sucking insects (Hemiptera), which include aphids, whiteflies, plant bugs and stink bugs, have emerged as major agricultural pests. The Hemiptera cause direct damage by feeding on crops, and in some cases indirect damage by transmission of plant viruses. Current management relies almost exclusively on application of classical chemical insecticides. While the development of transgenic crops expressing toxins derived from the bacterium Bacillus thuringiensis (Bt) has provided effective plant protection against some insect pests, Bt toxins exhibit little toxicity against sap sucking insects. Indeed, the pest status of some Hemiptera on Bt-transgenic plants has increased in the absence of pesticide application. The increased pest status of numerous hemipteran species, combined with increased prevalence of resistance to chemical insecticides, provides impetus for the development of biologically based, alternative management strategies. Here, we provide an overview of approaches toward transgenic resistance to hemipteran pests.

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Section: Plant Defense Proteins: Lectinsmentioning

confidence: 99%

Toxins for Transgenic Resistance to Hemipteran Pests

Chougule

Bonning

2012

Toxins

139

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“…Lectins are heterogenous group of proteins of non-immune origin possessing atleast one non-catalyic domain that specifically binds to carbohydrates. The physiological role of these lectins in plants is widely debated ranging from growth regulation (Howard et al, 1972), plant development (Brill et al, 2001), seed storage (Huang et al, 2006), and defense against pest and pathogen (Macedo et al, 2003;Luo et al, 2007). Among different lectins, lectins related to snowdrop lectin Galanthus nivalis agglutinin (GNA) have been well studied for its insecticidal property and several novel GNA like lectin genes were identified and characterized from different species of Alliaceae (Bandyopadhyay et al, 2001;Dutta et al, 2005;Chandrasekhar et al, 2014) and Araceae (Majumder et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Mannose-Binding Lectin Gene from Leaves of <I>Allium ascalonicum</I> (Shallot) and its Putative Role in Insect Resistance

Raja

Rajendran

Manoharan

et al. 2016

sijbs

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Plant lectins are the heterogenous group of glycoproteins extensively studied for their potent insecticidal property against Hemipteran pests. In this present study, the full-length cDNA of monocot mannose-binding insecticidal lectin gene was isolated from Allium ascalonicum leaves. The isolated Allium ascalonicum Lectin (AAL) gene was cloned in pGEM-T vector, sequenced and the sequence was submitted to GenBank (KM096570.1). Sequence analysis revealed a 468 bp open reading frame (ORF) encoding a putative 155 amino acids agglutinin precursor. Multiple sequence alignment and phylogenetic analysis of AAL amino acid with those of 30 other Mannose binding lectin (MBL) sequences in NCBI revealed a high similarity of 85-95% indicating that AAL is a member of the MBL super family and forms a cluster with other onion lectins. Secondary structure prediction and the homology modeling showed that AAL protein possess predominantly β-sheets and three potential mannose-binding motifs consisting of 5 amino acid residues QDNVY like other GNA lectins. The results of the insilico analysis predict that the Allium ascalonicum lectin gene can be another potent insecticidal protein.

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Fabrication and application of carbohydrate microarray for analyzing human serum antibody–carbohydrate interaction

Huang

Mei

Zhang

et al. 2006

Appl Microbiol Biotechnol

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We introduced a strategy for preparing a carbohydrate microarray and demonstrated its utility for characterizing carbohydrate binding and activities. We isolated the lipopolysaccharide (LPS) components from different bacteria and explored the possibility of immobilizing these glycoconjugates on a high-binding polystyrene plate. Carbohydrate-specific combination was examined by observing the binding of the blood group B analogic LPS O-polysaccharide from Escherichia coli on the high-binding polystyrene plate and anti-B from a broad spectra antibody of human blood serum. Strong binding of antibodies was screened, as it was evident that relative response value is two times higher than control. The hybridization results indicated that this method is a reliable technique for the detection of human intestinal bacteria and is expected to be applied in diagnostics and seroepidemiology.

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Structure-Function Relations of Carbohydrates by Neoglycolipid Arrays

Cited by 4 publications

References 9 publications

Toxins for Transgenic Resistance to Hemipteran Pests

Toxins for Transgenic Resistance to Hemipteran Pests

Isolation and Characterization of Mannose-Binding Lectin Gene from Leaves of <I>Allium ascalonicum</I> (Shallot) and its Putative Role in Insect Resistance

Fabrication and application of carbohydrate microarray for analyzing human serum antibody–carbohydrate interaction

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