Haemagglutinin activity in the haemolymph of Teleogryllus commodus (Walker)

Hapner, Kenneth D.; Jermyn, MA

doi:10.1016/0020-1790(81)90006-8

Cited by 39 publications

(15 citation statements)

References 16 publications

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“…However , the present results comes in contrast with the general characteristic of most C-type -lectins of T. commodus, M. sanguinipes, S. exigua, E. tiaratum, and nymph & adult S. gregaria (Hapner & Jermyn ,1981 ;Pendland & Boucias 1986 ;Stebbins & Hapner, 1985;Richards et al, 1988, Ayaad, 2004 ) that revealed a complete loss of HA in the presence of the strong chelator EDTA .…”

Section: Divalent Cation Requirementcontrasting

confidence: 99%

“…However, heat lability is characteristic for lectins of some other insects, e.g. the orthopterans T. commodus, (Hapner and Jermyn 1981), and M. sanguinipes (Stebbins and Hapner 1985), the dipteran Glossina fuscipes (Ingram and Molyneux, 1990) and the orthopteran S. gregaria (Ayaad,2004 andDorrah et al .,2009).…”

Section: Effects Of Induction and Blood Meal Feeding On Lectin Producmentioning

confidence: 99%

“…Most of the insect lectin isolated to date presents two different subunits with disulfide linkage, e.g., the mosquito Ae. stephensi (Chen and Billingsley, 1999), lectins of the orthopterans T. commodus (Hapner and Jermyn, 1981), M. sanguinipes (Stebbins and Hapner, 1985) and S. gregaria and the dictyopteran B. discoidalis (Chen et al, 1993). Group regions of resolution-enhanced 500-MHz 1 H NMR spectrum of Man 9 -GlcNAc 2 Asn component in D 2 O at 300 K .…”

Section: Molecular Characterization Of Cqlecmentioning

confidence: 99%

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Isolation of midgut agglutinin of Culex quinquefasciatus ( Diptera , Culicidae)

Ayaad

2009

Egyptian Academic Journal of Biological Sciences. A, Entomology

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A Lectin that agglutinates Eschrechia coli (ATCC 25922) , Staphylococcus aureus (ATCC 6538) live bacteria and various mammalian red blood cells (RBCs) was identified in Culex quinquefasciatus midgut extract (Cqlec) by using human (three groups: A, B, and O, RH+)mouse, rat, guinea-pig, rabbit and goat erythrocytes. With the use of (NH 4) 2 SO 4 fractionation, anion-exchange and GluNA-CBr-Sepharose 6B affinity chromatography, C. quinquefasciatus mid gut lectin has been purified to homogeneity. IEF and reducing SDS/PAGE revealed that the isolated mid gut lectin have isoelectric point (PI) of 6.30, and a subunit approximate molecular weight of 34.5 KDa .The highest agglutination activity of crude and isolated Cqlec were detected against both Eschrechia coli cells and rabbit RBCs. Significant differences in hemagglutinin titers and carbohydrate inhibition were detected between sugar fed and blood fed adult female mosquitoes.Overall agglutinin levels were increased following a blood meal feeding and E. coli induction using a hypodermic needle. This study presents the first report on the occurrence of heterogeneous anti rabbit RBC agglutinins in the midgut extracts of C. quinquefasciatus from Al kharj area in Saudi Arabia. The HA of lectins are Ca 2+ independent, heat-resistant, and are strongly inhibited by D(+)-mannose and D(+) glucose followed by N-acetyl-Dglucosamine. Raffinose and N-acetyl-D-manosamine were found to be moderate inhibitors. Non of the lectins were inhibited by galactose , lactose , trehalose or fetuin (1%) but the glycosubstances mucin and laminarin showed strong inhibitition using low concentrations. 2D-NMR spectroscopy revealed a component of the corresponding residue in structure having group regions of resolution spectrum of Man 9-GlcNAc 2 Asn.

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Section: Divalent Cation Requirementcontrasting

confidence: 99%

Section: Effects Of Induction and Blood Meal Feeding On Lectin Producmentioning

confidence: 99%

Section: Molecular Characterization Of Cqlecmentioning

confidence: 99%

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Isolation of midgut agglutinin of Culex quinquefasciatus ( Diptera , Culicidae)

Ayaad

2009

Egyptian Academic Journal of Biological Sciences. A, Entomology

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“…These lectins are of two types, an inducible type and a non-inducible type. In insects, inducible-type lectins are found in holometabolous insects [23 -251 and some non-inducible-type lectins are found in hemimetabolous insects [26,271. These lectins are supposed to participate in defence mechanisms or to be involved in coagulation of hemolymph.…”

Section: Discussionmentioning

confidence: 99%

Purification and some properties of a lectin from the hemolymph of Periplaneta americana (American cockroach)

Kubo

Natori

1987

Eur J Biochem

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A lectin showing specificity for human A‐type red blood cells was purified to homogeneity from the hemolymph of the American cockroach Periplaneta americana by affinity chromatography on bovine submaxillary gland mucin. This lectin was a huge molecule with molecular mass of about 1500 kDa, with a single subunit of 30‐kDa protein, and required Ca2+ for expression of lectin activity. Electron microscopic examination showed that these molecules were rods with helical structure with an average length of 50.5 nm and width of 10 nm. The molecule was suggested to contain tandemly aligned basic units of 10 nm length.

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“…The wells were mixed by pipetting and then kept at 4°C for 2 h. Agglutinated RBCs appeared to form a diffuse mat, whereas unagglutinated formed a clear dot on the bottom of the well. The HA was defined as the reciprocal of the maximum dilution of the test sample causing hemagglutination under the assay conditions (Hapner and Jermyn 1981;Ibrahim et al 1984).…”

Section: Hemagglutination Assay (Ha)mentioning

confidence: 99%

Isolation and Characterization of Midgut Lectin From Aedes aegypti (L.) (Diptera: Culicidae)

Ayaad

Al-Akeel

Olayan

2015

Braz. arch. biol. technol.

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The present investigation deals with the isolation and characterization of a lectin from Aedes aegypti (Ae aegypti) female mid gut extract that agglutinates various mammalian red blood cells (RBCs) human three groups A, B, and O (RH +), mouse, rat, guinea-pig, sheep and goat erythrocytes. The highest activity of both crude and isolated mid gut lectins were detected against sheep RBCs. Using (NH 4) 2 SO 4 fractionation, ion-exchange and mannose-CNBr-Sepharose 6B affinity chromatography techniques, Ae. aegypti midgut lectin (Aelec) was purified to homogeneity. Isoelectric focusing (IEF) and reducing SDS/PAGE revealed that the isolated mid gut lectin had isoelectric point (PI) of 5.90, and subunits approximate molecular weights of 35.50 and 27.35 KDa. The hemagglutination (HA) of lectins were Ca 2+-independent and heat-resistant. The sugar specificity of the purified Aelec was strongly inhibited by D (+)-mannose and raffinose, followed by D (+) glucose. N-acetyl-D-manosamine and N-acetyl-D-glucosamine were moderate inhibitors. None of the lectins were inhibited by the disaccharides such as galactose, lactose, trehalose (IC50 up to 200 mM or fetuin up to 1%) but the glycosubstances mucin and laminarin were strong inhibitors up to very low concentrations (0.030-0.003%).

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Haemagglutinin activity in the haemolymph of Teleogryllus commodus (Walker)

Cited by 39 publications

References 16 publications

Isolation of midgut agglutinin of Culex quinquefasciatus ( Diptera , Culicidae)

Isolation of midgut agglutinin of Culex quinquefasciatus ( Diptera , Culicidae)

Purification and some properties of a lectin from the hemolymph of Periplaneta americana (American cockroach)

Isolation and Characterization of Midgut Lectin From Aedes aegypti (L.) (Diptera: Culicidae)

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