Detection of blood group A-like substance in bacterial and viral vaccines by countercurrent immunoelectrophoresis using Helix pomatia lectin

We investigated localization of blood group antigens and their related substances in human labial salivary and submandibular glands by application of a post-embedding cytochemical staining procedure using lectin- or glycoprotein-gold complexes. Surgical tissue was obtained from 10 patients. Blood group-specific lectins, such as Dolichos biflorus agglutinin or Helix pomatia agglutinin (group A-specific), Griffonia simplicifolia agglutinin-I B4 (group B-specific), and Ulex europaeus agglutinin I (group H-specific) could recognize A, B, and H antigens, respectively, only in mature secretory granules (mature SG), which were found preferentially in cells in the late phase of the maturation cycle. In immature secretory granules (immature SG), which were found in cells in the early or middle phase of the maturation cycle, no binding with these lectins was observed. The Golgi complexes and endoplasmic reticula also were not labeled with these lectins. In blood group O and B secretors, blood group antigens were uniformly distributed throughout all the mature SG examined. However, in blood group A secretors, the distribution was heterogeneous, i.e., in some granules only H antigen was demonstrated, whereas in others both A antigens and a small amount of H antigens were detected. Among the blood group-nonspecific lectins, wheat germ agglutinin (WGA) was found to bind more preferentially to immature SG than to mature SG. This was demonstrated irrespective of the blood group and secretor status of the tissue donor, except that in blood group A secretors WGA bound strongly to some mature SG which possessed A antigen. We discuss the significance of cellular and subcellular mosaic distribution of blood group antigens in connection with morphological differences of secretory granules and the maturation cycle of mucous cells.

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Typing Blood Cells, One At A Time

Microscopy Today ◽

10.1017/s1551929500054602 ◽

2000 ◽

Vol 8 (7) ◽

pp. 3-7

Author(s):

Stephen W. Carmichael

Keyword(s):

Blood Group ◽

Human Blood ◽

Blood Cells ◽

Helix Pomatia ◽

Scanning Probe ◽

Active Molecule ◽

Blood Group A ◽

Atomic Force ◽

Group A ◽

Snail Helix Pomatia

We are all familiar with the 4 groups of human blood types; 0, A, B, and AB. Each group is characterized by specific molecules on the surface of the red blood cells (RBCs). Recently, Michel Grandbois, Wolfgang Dettmann, Martin Benoit, and Hermann Gaub have modified the atomic force microscope (AFM) to use the different affinities of these molecules to produce an image.A key step was to specifically functionalize the scanning probe tip of the AFM. What this means is to covalently attach an active molecule to the tip. The active molecule they used was a Iectin derived from the snail Helix pomatia (this is the same snail valued by the French as escargot). This Iectin binds specifically to molecules found on the surface of RBCs in blood group A (N-acetylgalactosamine-terminated glycolipids), but these molecules are not found in blood group O. But if the Iectin was bound directly to the AFM tip, nonspecific adsorption to the specimens would occur.

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The Action on Soluble Blood Group A Substances of an α-N-Acetylgalactosaminidase from Helix pomatia*

Biochemistry ◽

10.1021/bi00869a042 ◽

1966 ◽

Vol 5 (5) ◽

pp. 1742-1747 ◽

Cited By ~ 29

Author(s):

Hans Tuppy ◽

Walter L. Staudenbauer

Keyword(s):

Blood Group ◽

Helix Pomatia ◽

Blood Group A ◽

Group A

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Heterogeneity of Human Gallbladder Mucin in Bile

Clinical Science ◽

10.1042/cs0860067 ◽

1994 ◽

Vol 86 (1) ◽

pp. 67-74 ◽

Cited By ~ 10

Author(s):

Michel J. A. van Wijland ◽

J. Henriëtte Klinkspoor ◽

Laurens Th. de Wit ◽

Ronald P. J. Oude Elferink ◽

Guido N. J. Tytgat ◽

...

Keyword(s):

Blood Group ◽

Polyclonal Antibody ◽

Gallstone Disease ◽

Helix Pomatia ◽

Antigenic Determinants ◽

Human Gallbladder ◽

Blood Group A ◽

Helix Pomatia Agglutinin ◽

Significant Difference ◽

Group A

1. Human gallbladder mucin has been implicated to play a role in gallstone disease. In spite of this fact relatively little is known about the structure of human gallbladder mucin. In this study we have investigated the possible heterogeneity of mucin. For this purpose polyclonal and monoclonal antibodies against gallbladder mucin were raised. All antibodies reacted primarily with carbohydrate antigenic determinants. With these antibodies the immunoreactivity of gallbladder mucin from 60 patients with cholesterol gallstones and 20 subjects without stones was screened. In addition, reactivity with several lectins was studied. 2. Considerable heterogeneity was found with both antibody and lectin typing, but there was no significant difference in heterogeneity between mucin from patients with gallstones and control subjects. Immunoblotting revealed that there was similarity between the reaction of the polyclonal antibody and the Helix pomatia agglutinin. All mucin preparations reacting with the polyclonal antibody also bound to Helix pomatia agglutinin. Nineteen of the 21 reacting mucins (90%) were from patients with blood group A (18 patients) or AB (one patient) and expression of A antigen could be demonstrated on the mucin of these patients. The resulting two reacting mucins were from patients with type O. However, expression of the blood group antigen could not account for the lack of reactivity of the mucin of other patients. The Helix pomatia agglutinin partially blocked the reactivity of the polyclonal antibody, whereas anti-A antibody did not show inhibition, indicating that more then only blood group A epitopes were recognized by this antibody. 3. We conclude that considerable patient to patient heterogeneity of human gallbladder mucin exists. This may have functional consequences for the role of mucin in the pathogenesis of gallstone disease.

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