Preparation and properties of haemagglutinin from haemolymph of acrididae (Grasshoppers)

Stebbins, M. R.; Hapner, Kenneth D.

doi:10.1016/0020-1790(85)90057-5

Cited by 34 publications

(15 citation statements)

References 19 publications

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“…O n the basis of the SDS-PAGE findings, the M, value of approximately 65 kDa estimated for An.gamhiae midgut haemagglutinin was similar to that of the tsetse fly Glossirza palpalis (R-D.) 67 kDa midgut agglutinin, reported by Stiles et al (1990), and also to the haemolymph agglutinins isolated from Glossina fuscipes Newstead (Ingram & Molyneux, 1990) and the Orthopteran Melanoplus sanguinzpes (Stebbins & Hapner, 1985). However, the An.…”

Section: Discussionsupporting

confidence: 77%

Effects of physico‐chemical treatments on hemagglutination activity of Anopheles gambiae haemolymph and midgut extract

Mohamed

Ingram

1994

Medical Vet Entomology

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Anopheles gambiae midgut extracts and haemolymph possessed agglutinins, titre 1:16 to 1:256, against human red blood cells (RBCs). Subjection of both tissues to protein precipitation reagents, organic chemical and selected protease, neuraminidase and other glycosidic hydrolase treatments revealed the haemagglutinins to be protein, most likely glycoprotein, in nature--not lipoprotein, lipid, glycolipid or nucleic acid. An.gambiae agglutinins were thermo-labile > 40 degrees C, affected by freezing and thawing treatments, and contained disulphide and hydrogen bonds on the basis of sensitivity following exposure to dithiothreitol and urea respectively. Optimum haemagglutination depended generally on slightly acid to neutral pH conditions and agglutinin activity was Ca2+ ion, albeit to a lesser extent Mg2+ ion, dependent. The midgut extract agglutinin subunit molecule had a relative molecular weight (M(r)) of 65 kDa whilst that of haemolymph was 40 kDa. This study presents the first report on selected physico-chemical properties, the glycoproteinaceous nature and tentative subunit M(r) of mosquito midgut extract and haemolymph anti-RBC agglutinin(s).

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Section: Discussionsupporting

confidence: 77%

Effects of physico‐chemical treatments on hemagglutination activity of Anopheles gambiae haemolymph and midgut extract

Mohamed

Ingram

1994

Medical Vet Entomology

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“…Hemagglutinin activity has been reported in cell-free plasma fractions of the hemolymph of M. sanguinipes (Stebbins & Hapner, 1985;Hapner, 1983). We have demonstrated that the cell surface of the hemocytes from M. sanguinipes contain WGA-and ConA-binding sites.…”

Section: Resultsmentioning

confidence: 57%

“…One of the key interactions might involve fungal cell surface lectins (Latg6 et al, 1988), carbohydrates and glycoproteins (Hegedus etal., 1992;Hardham & Suzuki, 1990;Pendland etal., 1988 & Boucias, 1986) and receptors on the host hemocytes (Miranpuri etal., 1992;Pendland et al, 1988). Hemagglutinin activity has been reported in cell-free plasma fractions of the hemolymph of M. sanguinipes (Stebbins & Hapner, 1985;Hapner, 1983). Additionally, this glycoprotein is present on our B. bassiana strain regardless of growth medium composition and type of culturing (i.e., submerged or solid state).…”

Section: Resultsmentioning

confidence: 63%

“…The occurrence and hemagglutination characteristics of hemolymph hemagglutinin activity have been reported in several acridid species including grasshoppers (Stebbins & Hapner, 1985;Hapner, 1983;Jurenka etal., 1982). Pendland and Boucias (1986) have shown that the hyphomycetous insect pathogens Nomuraea rileyi, Paecilomyces farinosus, Metarrhizium anisopliae and B. bassiana have Con A and WGA reactive surface sugars, i.e., glucose, mannose, N-acetyl-D-galactosamine (GlacNAc) and GluNAc.…”

Section: Introductionmentioning

confidence: 99%

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Hemocyte surface changes in the migratory grasshopper, Melanoplus sanguinipes in response to wounding and infection with Beauveria bassiana

Miranpuri

Khachatourians

1993

Entomologia Exp Applicata

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Surface changes of hemocytes from the migratory grasshopper, Melanoplus sanguinipes (Fab.), following wounding and/or infection with Beauveria bassiana (Bals.) Vuillemin were assessed using fluorescein labelled wheat germ agglutinin (WGA) and concanavalin A (Con A). Binding was observed on outer wall of hemocytes when either Con A or WGA conjugates were tested. After infection there was an increase in the percentage of hemocytes which bound to WGA and which remained so for 24 h. However, after wounding this increase in binding subsided after only 1 h. Furthermore, it was found that the increase in WGA-binding occurred within the first 15 min of wounding or infection. In addition, ConA binding in males only increased 3-fold in fungus-injected insects within 1 h of treatment and remained high for 24 h. These results indicated the presence of mannose (and/or glucose) residues (Con A specificity) and N-acetyl-D-glucosamine residues (wheat germ agglutinin; WGA specificity) on outer wall surfaces of the hemocytes. The implications of these results in the immune response of M. sanguinipes to infection with B. bassiana are discussed.

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“…Their functions, however, are not fully understood. Some lectins are supposed to participate in embryonic development (Beyer and Barondes 1982;Roberson and Barondes 1982), and others are thought to be involved in defence mechanisms (Parish 1977;Stebbins and Hapner 1985). In Sarcophaga peregrina, a galactose-binding lectin from haemolymph was purified and characterized extensively (Komano et al 1980(Komano et al , 1983(Komano et al , 1987.…”

Section: Introductionmentioning

confidence: 99%

Involvement of a maternally transcribed lectin gene in the early development of Bombyx mori

Amanai

Suzuki

Ohtaki

1994

Roux's Arch Dev Biol

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The expression of a lectin gene was investigated during oogenesis and embryonic development of the silkworm, Bombyx mori. During oocyte development, the Bombyx 50 kDa lectin gene was transcribed in the nurse cells, the transcripts were transferred through the ring canal from the nurse cell cytoplasm to the ooplasm, and were deposited in the ooplasm cortex. In unfertilized eggs the transcripts were restricted to the cortex, the site of formation of cells in the embryo. In early embryos the transcript and its products only accumulated in the serosa cell cytoplasm and little of the lectin was deposited in other egg regions such as the germ-band. These patterns of localization suggest that this lectin plays a part in serosa formation in early embryogenesis in a maternal effect manner.

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Preparation and properties of haemagglutinin from haemolymph of acrididae (Grasshoppers)

Cited by 34 publications

References 19 publications

Effects of physico‐chemical treatments on hemagglutination activity of Anopheles gambiae haemolymph and midgut extract

Effects of physico‐chemical treatments on hemagglutination activity of Anopheles gambiae haemolymph and midgut extract

Hemocyte surface changes in the migratory grasshopper, Melanoplus sanguinipes in response to wounding and infection with Beauveria bassiana

Involvement of a maternally transcribed lectin gene in the early development of Bombyx mori

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