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PubMed1975

The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea).

Peanut agglutinin was purified by affinity chromatography on Sepharose-epsilon-aminocaproyl-beta-D-galactopyranosylamine. The purified lectin obtained in a yield of 150 mg/100 g of defatted peanut was homogeneous on polyacrylamide gel electrophoresis, ultracentrifugation, and gel filtration. This intrinsic sedimentation coefficient (So20,w) and the intrinsic diffusion coefficient (Do20,w) were estimated at pH 7.4 as 5.7 +/- 0.1 S and 5.0 X 10(-7) cm2s(-1), respectively. The molecular weight of the agglutinin, determined by sedimentation and diffusion and by gel filtration, was found to be 110,000. Disc gel electrophoresis and gel filtration, both in the presence of sodium dodecyl sulfate, gave a single component of Mr = 27,500 suggesting that the lectin is a tetramer composed of four subunits. Four alanine residues per 110,000 g were found by NH2-terminal analysis and the sequence of the five NH2-terminal amino acids was: ALa-Glu-Ser-Val-Thr. Each cycle in a sequenator gave a single amino acid, suggesting that the four subunits are identical. Peanut agglutinin does not contain covalently bound sugar; it is devoid of cysteine and cystine, low in methionine, histidine, and tryptophan, but rich in acidic and hydroxyamino acids. The lectin agglutinated erthrocytes of human ABO blood types equally well, but only after they have been treated with neuraminidase. Of the monosaccharides tested for inhibition of hemagglutination only D-galactose and alpha- and beta-D-galactosides were active. High inhibitory activity was found with the Discaccharide DGalbeta(1 in equilibrium 3)DGalNAc and with the disialylated glycoproteins: alpha1-acid glycoprotein, fetuin, glycophorin, and human blood group NN or MM antigen. These desialylated glycoproteins also reacted with the lectin to form precipitin bands in Ouchterlony double diffusion in agar.

Amino Acid Sequence↗
PubMedDate not supplied

Immunoaffinity column as cleanup tool for a direct competitive enzyme-linked immunosorbent assay of cyclopiazonic acid in corn, peanuts, and mixed feed.

An immunoaffinity column (IAC) for cyclopiazonic acid (CPA) was prepared by coupling a CPA-specific monoclonal antibody to CNBr-activated sepharose 4B. A direct competitive enzyme-linked immunosorbent assay (dc-ELISA) was used to study the chromatographic behavior of a 0.2 mL gel column with a binding capacity of 4 micrograms CPA/column as well as to evaluate its efficacy as a cleanup tool for analysis of naturally occurring CPA. Sample extract either in buffer solution or in a solution containing up to 35% methanol could be loaded onto the column. After the column is washed with 5 mL deionized water and 5 mL 50% methanol, CPA could be quantitatively eluted with 2 mL 100% methanol. The column could be regenerated at least 10 times by washing with 10 mL equilibrating buffer and then storing in a cold room overnight before reuse. Recoveries of CPA added to corn, peanut, and mixed feed extracts in the range 10-200 ng/g were 88-105, 86-100, and 90-110%, respectively. Detection limits were 2.0, 4.4, and 4.7 ng/g for corn, mixed feed, and peanuts, respectively. Twenty-two peanut samples naturally contaminated with CPA were subjected to both IAC and solvent partition cleanup followed by dc-ELISA. Although a good correlation between data obtained from IAC-dc-ELISA and from SP-dc-ELISA (r = 0.75, p < 0.0001) was obtained, the slope of the linear regression was low (0.67), indicating loss during solvent partition cleanup. The overall data showed that the combination of IAC and dc-ELISA is an effective method for CPA analysis.

Animal Feed↗
PubMed1990

Absorption of a pharmacological dose of vitamin D3 from two different lipid vehicles in man: comparison of peanut oil and a medium chain triglyceride.

The absorption of a pharmacological dose of vitamin D3 from two different lipid vehicles, peanut oil, containing long chain fatty acids, and a medium chain triglyceride was compared. Serial measurements of the serum concentration of vitamin D3 after dosage were made. The serum levels of 25-hydroxyvitamin D3, the major circulating vitamin D3 metabolite, were also determined. The analytical methods used were based on HPLC. In the fasting state, the serum levels of vitamin D3 were significantly higher after administration in peanut oil than after administration in the medium chain triglyceride. When the vitamin D3 dose was ingested together with food no difference between the two formulations was observed. Only small inter-formulation differences in serum 25-hydroxyvitamin D3 levels were detected. The results indicate that the presence of long chain fatty acids facilitates the absorption of vitamin D3.

Adult↗
PubMed1987

Cytostructural localization of peanut lectin binding in fine-needle aspirates of benign and malignant breast lesions.

Numerous studies have employed lectin binding patterns to investigate alterations in cell surface polysaccharide expression associated with malignant transformation. Cytostructural relocalization of peanut lectin (Arachis hypogaea) binding sites from the cell surface to the cytoplasm has been described in breast carcinomas. To investigate the possible utility of peanut lectin binding patterns in the diagnosis of breast fine-needle aspirations, the PNA immunoperoxidase method was applied to smears from a group of 15 benign and malignant breast lesions. Cytostructural relocalization of PNA binding was seen in both benign and malignant breast lesions, indicating that it is of little diagnostic utility in the assessment of malignancy. This finding was noted in both cytologic and histologic preparations.

Binding Sites↗
PubMed1985

Visualization of the secretory canaliculi of human parietal cells with a peroxidase-labelled peanut lectin. Light- and electron-microscopic observations.

Peanut lectin reactivity was examined in normal fundic glands from human gastric samples, both at light- and electron-microscopic levels, using a peroxidase conjugate. Positive reaction was observed in the glycocalyx of parietal cell secretory canaliculi as well as in the mucous globules of mucous cells and in the luminal cell coat of chief cells. The presence of terminal galactose in the canalicular glycocalyx may be connected with the peculiar function of hydrochloric acid secretion. Peroxidase-labelled peanut lectin is proposed as a marker for visualizing the secretory canaliculus of parietal cells.

Galactose↗
PubMed1989

Early development of the representation of the body surface in SI cortex barrel field in neonatal rats as demonstrated with peanut agglutinin binding: evidence for differential development within the rattunculus.

Physiological studies have demonstrated a highly organized somatotopic representation of the body surface in SI cortex of rat. This representation is correlated morphologically with the presence of barrel-shaped structures in layer IV. Conventional staining techniques reveal barrels in the latter part of the first postnatal week. Recently, the peroxidase conjugates of lectins, which recognize glycosylated molecules, have been used to study barrel field formation. Con A, for example, has been shown to bind primarily to prospective barrel sides and septa as early as postnatal day 3 (PND-3) in mouse. To date, investigations of SI cortex using the lectin (Arachis hypogaea) peanut agglutinin (PNA) have been confined to the study of the barrel field representation of the face and mystacial vibrissae in the mouse. In the present study we extend these findings to the development of the representation of the entire body surface called the rattunculus. Rats ranging from PND-1 (first 24 h after birth) to PND-12 were anesthetized with Nembutal and perfused with 4% paraformaldehyde and 2% glutaraldehyde in 0.2 M sodium cacodylate buffer. Brains were removed, flattened tangentially, and sectioned on a vibratome at 30-120 microns. Sections were blocked in TRIS-buffered saline (TBS) plus 2% bovine serum albumin and incubated in peanut lectin at 4 degrees C. Following incubation, sections were washed with TBS and processed using peroxidase histochemistry. Lectin binding in the prospective forelimb representation was apparent by PND-5 whereas lectin binding to the prospective face-mystacial vibrissae representation occurred before PND-4. These results suggest that body part representations show individual variations during early pattern formation.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1984

Peanut lectin histochemistry of 120 mammary carcinomas and its relation to tumor type, grading, staging, and receptor status.

Peanut lectin (PNL) is known to bind beta-D-galactosyl-(1-3)-N-acetyl-D-galactosamine, which provides antigenic determination of the Thomsen-Friedenreich antigen ( TFAg ). The aim of this study was to analyse the expression of peanut lectin binding sites in mammary carcinomas and to correlate these with tumor type, histological grading, staging and biochemical receptor status. The series comprised 120 invasive mammary carcinomas and 14 cases with normal breast tissue or benign epithelial proliferations as controls. In controls mainly luminal or apical PNL-binding was discovered, however, in all except three carcinomas a cytoplasmatic localisation of TFAg with three major patterns was found: diffuse, granular-globular and vacuolar reactions. The quantitative-qualitative evaluation of the PNL-staining revealed a statistically significant correlation between globular-vacuolar PNL-reaction and tumor type with a higher percentage of this type of reaction in invasive lobular carcinomas as opposed to tubular and invasive ductal carcinomas. Furthermore a statistically significant relationship was disclosed between PNL- histopositivity and estrogen positive - progesterone positive cases. However, the findings of contradictory PNL-status and hormone-receptor status illustrates clearly the difficulty of predicting the biochemical receptor status. No correlation was found between PNL-histochemistry, histological grading, and pathological staging. The practical implications of PNL-histochemistry of mammary carcinomas are discussed.

Arachis↗
PubMed1989

Nutritional evaluation of experimental weaning foods prepared from green leaves, peanut oil, and legume flour.

Experimental weaning foods were prepared from alfalfa leaves, peanut oil, and mung bean, chickpea or soy flour. The weaning foods were analyzed to determine their yield, proximate composition and amino acid content. Yields from starting materials ranged from 29 to 99%. Highest yields were obtained when 20% legume or oilseed flour was incorporated into leaf protein-peanut oil gels. The moisture content of the weaning foods ranged from 42 to 65%, protein from 3.4 to 6.5%, fat from 23 to 48%, and carbohydrate from 3 to 13%. Proteins in the experimental weaning foods were found to be deficient in the sulfur amino acids. Amino acid scores for weaning foods containing 20% legume or oilseed flour ranged from 50 for mung bean to 62 for soy. It was estimated that a four-ounce daily serving of one of the soy weaning foods would supply 40% of the energy and 35% of the protein needs of a one-year-old infant.

Amino Acids↗
PubMed1985

T-antigen expression by peanut agglutinin staining relates to mucosal dysplasia in ulcerative colitis.

Staining of 326 rectal mucosal biopsies from ulcerative colitis patients with peanut agglutinin (PNA), which binds to the T-blood group antigen and has been claimed to reflect a cancer-associated mucin alteration, showed highly significant direct associations with mucosal dysplasia (P less than 0.001), disease activity (P less than 0.001), and subsequent development of rectal cancer in a smaller series of patients (P = 0.005). Staining for normal colonic mucin by the Dolichos biflorus (DBA) lectin related significantly and inversely to dysplasia. Intense normal colon mucin staining by DBA related significantly (P less than 0.025) to long disease duration and to subsequent development of cancer (P = 0.02). The latter association is based on a small number of patients only and is not considered conclusive evidence, but may provide a link with goblet-cell hyperplasia. The authors conclude that although T-antigen expression relates to dysplasia, the findings of "false" positive and negative rates of 22 and 33 percent respectively, make it unlikely that staining of biopsy sections for the T-antigen by peanut agglutinin will contribute materially to routine assessment for dysplasia and cancer risk prediction in patients with ulcerative colitis.

Adult↗
PubMed1982

Influence of native and randomized peanut oil on lipid metabolism and aortic sudanophilia in the vervet monkey.

Vervet monkeys (Cercopithecus aethiops pygerethrus) were fed cholesterol-free, semipurified diets containing 40% sucrose, 25% casein, 15% cellulose and 14% peanut oil (PNO), randomized peanut oil (RPNO) or corn oil (CO). After 4 months, serum cholesterol and triglyceride levels, serum lecithin-cholesterol acyl transferase (LCAT) activity and plasma lipoprotein lipase (LPL) activity were similar in all groups. Livers of monkeys fed CO converted 156% more acetate and 24% more mevalonate to cholesterol than those of monkeys fed RPNO. Cholesterogenesis in RPNO-fed monkeys was enhanced compared to PNO (68% from acetate; 62% from mevalonate). Incidence of atherosclerosis was 33% in monkeys fed RPNO, 80% in those fed CO and 90% in those fed PNO. Extent of sudanophilia was lowest in aortas of monkeys fed RPNO. Incidence of arteriosclerosis was 40% in monkeys fed CO, 56% in those fed RPNO and 70% in those fed PNO. Extent of aortic surface showing arteriosclerosis was highest in monkeys fed RPNO.

Animals↗
PubMed1983

Binding of FITC-coupled peanut-agglutinin (FITC-PNA) to embryonic chicken retinas reveals developmental spatio-temporal patterns.

FITC-labeled peanut agglutinin (PNA), a lectin from peanut (Arachis hypogaea) which binds specifically to D-galactose, was used as a probe to trace the distribution of PNA-lectin receptors during early development of chick retina. We found that specific fluorescence within the inner plexiform layer (IPL) and the outer plexiform layer (OPL) appears at different developmental stages. The specific fluorescence of the IPL first appears near the central area of the ventro-posterior quadrant of the 7-day retina, then extends progressively towards the periphery, reaching the ora serrata earlier on the posterior than on the anterior side. The development of the specific fluorescence of the OPL follows the same scheme, but it appears later (starting at day 9) than that of the IPL and it is less pronounced. The spatio-temporal patterns of the expression of the lectin receptors show relationships to those of withdrawal of proliferating cells from mitosis, and of other events related to differentiation.

Animals↗
PubMed1992

Isolation and characterization of a lectin from peanut roots.

A glucose-specific lectin has been purified to apparent homogeneity from 7-day-old peanut (Arachis hypogaea) roots by affinity chromatography on a Sephadex G-50. The lectin has a 66 kDa native molecular mass and a 33 kDa subunit molecular mass as revealed by native and denaturing sodium dodecyl sulphate-polyacrylamide gel electrophoresis, respectively. The purified lectin, gives a single precipitin line with the antiserum produced against 7-day-old root extract and shows 5 bands in the pH range of 4.4-5.4 in the isoelectric focusing gel. The glucose-specific lectin activity in the peanut roots appears from the fourth day onwards. Lipopolysaccharides isolated from the host specific Rhizobium strain are a 68-fold more potent inhibitor of the lectin as compared to glucose.

Animals↗
PubMed2004

Microarray immunoassay: association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes.

BACKGROUND: IgE epitope mapping of food allergens is a prerequisite for engineering hypoallergenic immunotherapeutic agents and might reveal basic information regarding a patient's immune response. Mapping of large numbers of epitopes by using individual patient sera has been impractical with current techniques. OBJECTIVE: We sought to develop a peptide microarray-based immunoassay to map peanut epitopes by using microliter quantities of serum. METHODS: A set of 213 overlapping 20-residue peptides was synthesized corresponding to the primary sequences of Ara h 1, Ara h 2, and Ara h 3. These were arrayed in triplicate along with the corresponding recombinant proteins onto glass slides and used for immunolabeling. RESULTS: Seventy-seven patient and 15 control sera were analyzed. The majority of patients (97%) had specific IgE to at least one of the recombinant allergens, and 87% had detectable IgE to sequential epitopes. Microarray mapping correlated well with previous studies. However, the analysis of individual patients revealed remarkable heterogeneity in the number and patterns of epitope recognition. High epitope diversity was found in patients with a history of more severe allergic reactions. Also, sensitization of effector cells with more diverse IgE antibodies conferred greater reactivity to specific allergen. CONCLUSIONS: The protein microarray immunoassay confirmed that Ara h 1, Ara h 2, and Ara h 3 are major peanut allergens and allows for parallel epitope analysis. This has led to the discovery of an additional important epitope of Ara h 1 and the recognition of a high degree of patient heterogeneity. This qualitative difference in epitope diversity might provide prognostic information about the patient.

2S Albumins, Plant↗
PubMed2005

IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen, Ara h 2.

BACKGROUND: Detailed assessment of antibody responses to allergens reveals clinically relevant information about both host response and antigen structure. Microarray technology offers advantages of scale and parallel design over previous methods of epitope mapping. OBJECTIVE: We designed a redundant peptide microarray for IgE and IgG4 epitope mapping of the previously characterized peanut allergen, Ara h 2. METHODS: Six complete sets of overlapping peptides were commercially synthesized and site-specifically bound to epoxy-derivatized glass slides in triplicate. Peptides were 10, 15, or 20 amino acids in length with an offset of either 2 or 3 amino acids. A total of 10 control and 45 peanut-allergic sera were assayed. Specific IgE and IgG4 were detected by using fluorochrome-labeled monoclonal secondary antibodies. RESULTS: By using 15-mer and 20-mer peptides, we could define 11 antigenic regions, whereas only 5 were identifiable using 10-mers. Controls and patients produced IgG4 recognizing a comparable number of Ara h 2 peptides, although the dominant epitopes were distinct. As expected, patient IgE bound a larger number of Ara h 2 peptides (9.4% vs 0.9%). IgE and IgG4 epitopes recognized by patients were largely the same, and there was a positive association between IgE and IgG(4) signal, suggesting coordinate regulation. Cluster analysis of peptide binding patterns confirmed the specificity of antibody-peptide interactions and was used to define 9 core epitopes ranging from 6 to 16 residues in length-7 of which (78%) agreed with previous mapping. CONCLUSION: Epitope mapping by microarray peptide immunoassay and cluster analysis reveals interpatient heterogeneity and a more detailed map.

2S Albumins, Plant↗
PubMed2026

Genome-wide identification of the peanut HD-Zip gene family and AhHDZ15 positively regulating salt and drought stress in heterologously overexpressed Arabidopsis.

Homeodomain-leucine zipper (HD-Zip) transcription factors play important roles in plant growth, development, and abiotic stress responses. However, bioinformatic analyses and functional studies of HD-Zip family in peanut are scarce. In this study, 128 AhHDZ genes were identified and classified into four subfamilies in the phylogenetic analysis. Transcriptomic data and RT-qPCR analysis indicated the expression levels of AhHDZ4 and AhHDZ15 were significantly elevated in response to 12&#x202f;h of salt stress, while AhHDZ4/15/60/69/126 all showed a progressive increase over time in response to drought stress. AhHDZ15 protein was localized in the nucleus. Under salt and drought stress, the germination rates of AhHDZ15-overexpressing in Arabidopsis were significantly higher than wild-type (WT), and root lengths were also significantly longer than WT. In addition, the SOD, CAT, chlorophyll content, and Relative Leaf Water Content (RLWC) value of leaves in AhHDZ15-overexpressing lines were significantly higher than WT, while the MDA content was significantly lower than WT. The above results indicate that heterologous overexpression of AhHDZ15 enhanced salt and drought tolerance in Arabidopsis. Furthermore, AhHDZ15 could bind to the L1-box element of the AhVNI2 promoter, thereby activating AhVNI2 transcription and enhancing the expression of downstream salt stress-responsive genes. These findings implies a potential function of AhHDZ15 in peanut that requires further validation.

Arabidopsis↗
PubMed1998

Interaction of peanut root lectin (PRA II) with rhizobial lipopolysaccharides.

Sugar specific binding of peanut root lectin (PRA II) to peanut specific bradyrhizobial lipopolysaccharides (LPS) was demonstrated by gel retardation assay and lectin based ELISA. Sephadex G-50 gel purified high molecular weight polysaccharides from NC 92 LPS bind PRA II most efficiently. Binding of NC 92 LPS only to PRA II and not to PNA, SBA and PSL by Western blot analysis suggests that this lectin-LPS interaction is tissue as well as species specific.

Enzyme-Linked Immunosorbent Assay↗
PubMed2002

Stochastic molecular dynamics of peanut lectin PNA complex with T-antigen disaccharide.

The stochastic boundary molecular dynamics simulation method was applied to investigate the structure of a complex comprised of a tetrameric peanut lectin and the tumour-associated disaccharide, Galbeta1-3GalNAc (T-antigen). Only a small region encompassing the active site was explicitly included in the calculations, but the electrical contribution of most outer atoms was taken into account by adding to the effective potential a term coming from an electrostatic potential grid that was pre-calculated and used to approximate the electrostatic energy and the force at any point in the interacting site. Results of simulating the intermolecular hydrogen bond network agree fairly well with X-ray experiments. An estimation of the direct and water-mediated interaction mean lifetimes and mean water residence times around the T-antigen oxygen atoms was computed over 400 ps. Monitoring the behaviour of water molecules within the active site revealed that there is a constant exchange of water with the bulk, especially in the proximity of ASN41, ASN127 and GLU129. The temporal evolution of the glycosidic linkage was also investigated and compared with simulations of T-antigen in solution. These studies of peanut lectins-sugar complexes clearly emphasize the importance of bound water molecules in generating carbohydrate specificity.

Antigens, Tumor-Associated, Carbohydrate↗
PubMed2001

Mutational analysis at Asn-41 in peanut agglutinin. A residue critical for the binding of the tumor-associated Thomsen-Friedenreich antigen.

Peanut agglutinin is a clinically important lectin due to its application in the screening of mature and immature thymocytes as well as in the detection of cancerous malignancies. The basis for these applications is the remarkably strong affinity of the lectin for the tumor-associated Thomsen-Friedenreich antigen (T-antigen) and more so due to its ability to distinguish T-antigen from its cryptic forms. The crystal structure of the complex of peanut agglutinin with T-antigen reveals the basis of this specificity. Among the contacts involved in providing this specificity toward T-antigen is the water-mediated interaction between the side chain of Asn-41 and the carbonyl oxygen of the acetamido group of the second hexopyranose ring of the sugar molecule. Site-directed mutational changes were introduced at this residue with the objective of probing the role of this residue in T-antigen binding and possibly engineering an altered species with increased specificity for T-antigen. Of the three mutants tested, i.e. N41A, N41D, and N41Q, the last one shows improved potency for recognition of T-antigen. The affinities of the mutants can be readily explained on the basis of the crystal structure of the complex and simple modeling. In particular, the change of asparagine to glutamine could lead to a direct interaction of the side chain with the sugar while at the same time retaining the water bridge. This study strengthens the theory that in lectins the nonprimary contacts generally made through water bridges are involved in imparting exquisite specificity.

Antigens, Tumor-Associated, Carbohydrate↗