A Monoclonal Antibody and the Lectin Wheat Germ Agglutinin Induce Zoospore Encystment in Pythium porphyrae, a Marine Microbial Pathogen

Mycologia ◽  
2002 ◽  
Vol 94 (4) ◽  
pp. 712 ◽  
Author(s):  
M. K. Addepalli ◽  
Yuji Fujita ◽  
Kinya Kanai
Keyword(s):  
Monoclonal Antibody ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Pythium Porphyrae ◽  
Microbial Pathogen

scholarly journals Wheat germ agglutinin induces mating reactions in Chlamydomonas eugametos by cross-linking agglutinin-associated glycoproteins in the flagellar membrane.

1989 ◽  
Vol 109 (4) ◽  
pp. 1677-1687 ◽  
Author(s):  
R Kooijman ◽  
P de Wildt ◽  
S Beumer ◽  
G van der Vliet ◽  
W Homan ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Specific Binding ◽  
Cross Linking ◽  
Intracellular Signals ◽  
Chlamydomonas Eugametos ◽  
Species Specific ◽  
Generating System ◽  
Binding Glycoprotein

Species-specific binding between the flagellar surfaces of mating types plus and minus (mt+ and mt-) gametes of Chlamydomonas eugametos is mediated by mating type-specific agglutinins. Their interaction triggers several mating responses that are necessary for cell fusion, such as flagellar twitching, flagellar tip activation, redistribution of agglutinin molecules to the flagellar tip (tipping), and mating structure activation. Earlier, we reported that a monoclonal antibody (mAb 66.3) can induce mating reactions by cross-linking the agglutinins (Homan, W. L., A. Musgrave, H. de Nobel, R. Wagter, A. H. J. Kolk, D. de Wit, and H. van den Ende. 1988. J. Cell Biol. 107:177-189). Here we report that the lectin wheat germ agglutinin (WGA), which does not bind to the agglutinins, can also invoke all these mating reactions. We show, by immunofluorescence studies using anti-WGA and an agglutinin-specific monoclonal antibody (mAb 66.3), that WGA induces the redistribution of agglutinin to the flagellar tips of mt- gametes. Vice versa, when agglutinin tipping is induced by mAb 66.3, the WGA-binding glycoproteins are also tipped. Under the same conditions, the major flagellar glycoproteins are not redistributed, indicating that membrane transport is limited to a few components. We conclude that each agglutinin is associated with a WGA-binding glycoprotein. When cells lacking agglutinin or cells possessing inactive agglutinins are treated with WGA, mating responses are again elicited. The data suggest that clustering of agglutinin-containing complexes results in the production of intracellular signals, such as cAMP, and the coupling of the complex to a force generating system. In nature, the complexes are clustered via the agglutinins, but artificially they can be clustered by lectins or antibodies directed against other proteins in the complex.

Failure of 6D1 or Exposure of Platelets to ADP to Affect Agglutination Induced by Wheat Germ Agglutinin

1989 ◽  
Vol 62 (02) ◽  
pp. 815 ◽  
Author(s):  
Marjorie B Zucker ◽  
Robert A Grant ◽  
Evelyn A Mauss
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ

Transport Characteristics of Wheat Germ Agglutinin-Modified Insulin-Liposomes and Solid Lipid Nanoparticles in a Perfused Rat Intestinal Model

2006 ◽  
Vol 6 (9) ◽  
pp. 2959-2966 ◽  
Author(s):  
Na Zhang ◽  
Qineng Ping ◽  
Guihua Huang ◽  
Xiuzhen Han ◽  
Yanna Cheng ◽  
...  
Keyword(s):  
Solid Lipid Nanoparticles ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Serum Insulin ◽  
Lipid Nanoparticles ◽  
Solid Lipid ◽  
Mucosal Absorption ◽  
Perfusion Experiment ◽  
Absorption Sites

Wheat germ agglutinin (WGA) modified liposomes and solid lipid nanoparticles (SLNs) were evaluated for improving intestinal absorption of insulin. In an in situ local intestinal perfusion experiment, formulations containing 100 IU/kg insulin were administered to the duodenum, jejunum, and ileum of fasted rats. As hypothesized, ileum was the best intestinal location for the absorption of insulin-containing liposomes. Serum insulin concentrations decreased for the various formulations in different absorption sites according to the following trends: Duodenum > ileum > jejunum for WGA-modified insulin-containing liposomes; duodenum > jejunum > ileum for WGA-modified insulin-containing SLNs; ileum > jejunum > duodenum for insulin-containing liposomes; ileum > duodenum > jejunum for insulin-containing SLNs; and duodenum ≥ ileum > jejunum for aqueous solution of insulin. These results imply that the nanoparticle type and delivery site were important factors with respect to increasing the bioavailability of insulin following oral administration. The proteolytic degradation as well as the epithelial permeability were primary determinants influcing insulin mucosal absorption.

Identification of distinct haemocyte populations from the freshwater bivalves swan mussel (Anodonta cygnea) and duck mussel (Anodonta anatina) using wheat-germ agglutinin

2017 ◽  
Vol 95 (12) ◽  
pp. 937-947 ◽  
Author(s):  
M. Hinzmann ◽  
M. Lopes-Lima ◽  
F. Cerca ◽  
A. Correia ◽  
J. Machado ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Transmission Microscopy ◽  
Anodonta Cygnea ◽  
Functional Studies ◽  
Lectin Staining ◽  
Surface Staining ◽  
Cytological Features ◽  
Freshwater Bivalves

Haemocytes play a major role in molluscs immunity. Functional studies are, however, impaired by limited available experimental tools to identify and sort distinct haemocyte populations. Therefore, using nonlethal methods, we aimed at evaluating whether lectin staining combined with flow cytometry could be used to distinguish circulating haemocyte populations from two freshwater bivalves of the family Unionidae, the duck mussel (Anodonta anatina (L., 1758)) and the swan mussel (Anodonta cygnea (L., 1758)). Based on classical classification, haemocytes were distinguished as granulocytes and hyalinocytes and cytological features were visualized using transmission microscopy and staining techniques. Size, granularity, viability, and surface staining using lectins as specific probes were analysed by flow cytometry and fluorescence microscopy. The microscopic proportions of granulocytes and hyalinocytes significantly differed, being of 70% and 30% for A. cygnea and of 85% and 15% for A. anatina, respectively. Two haemocyte populations were sorted by flow cytometry based on size and granularity and confirmed as granulocytes and hyalinocytes. Interestingly, two different granulocyte populations could be further discriminated in A. cygnea according to their binding affinity to wheat-germ agglutinin (WGA), whereas granulocytes of A. anatina all stained similarly. Our results show that WGA labelling combined with flow cytometry can be used to better discriminate Anodonta haemocyte populations and obtain purified populations for functional studies.

Protein phosphorylation and activation of platelets by wheat germ agglutinin

1985 ◽  
Vol 132 (1) ◽  
pp. 313-319 ◽  
Author(s):  
Chhanda L. Ganguly ◽  
Mohanathasan Chelladurai ◽  
Pankaj Ganguly
Keyword(s):  
Protein Phosphorylation ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ
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