Blood-Group and Forssman Antigenic Determinants Shared between Microbes and Mammalian Cells1

Author(s):  
G. F. Springer
1982 ◽  
Vol 60 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Raymond U. Lemieux ◽  
Maria Halina Burzynska

In order to investigate the immunological properties of certain I blood group specific glycoproteins, the potential antigenic determinants βDGlcNAc(1 → 6)αDGalNAc and βDGal(1 → 4)βDGlcNAc(1 → 6)αDGalNAc attached as glycosides to 8-methoxy-carbonyloctanol were synthesized by way of the phthalimido-chloride method.


2020 ◽  
Vol 65 (4) ◽  
pp. 216-221
Author(s):  
Frida Nasyrovna Gilmiyarova ◽  
N. A. Kolotyeva ◽  
V. I. Kuzmicheva ◽  
O. A. Gusyakova ◽  
I. A. Borodina ◽  
...  

AB0 blood group antigens were discovered over a century ago; however, it is still important to study their role in development of various pathological conditions. Today it is known that antigenic determinants of this blood group are present not only on erythrocyte membrane but also on other cells and tissues: platelets, gastrointestinal epithelium and salivary glands, respiratory system cells. In the last decade, a large number of studies have appeared to reveal the relationship between a specific disease and blood group type, meta-analyses have been published. Previously, the authors have studied the metabolic status, cell composition and coagulation profile of clinically healthy individuals for more than on 180,000 donations, that allowed to identify group-specific features for each blood group. This review presents generalized data on the association of such pathological conditions as coronary heart disease, thromboembolic complications, tumors of various localizations, inflammatory and destructive oral diseases, psychiatric and some infectious diseases with the presence or absence of antigenic determinants A and B. Carriers of blood group 0 (I) are generally more resistant to diseases, with the exception of H.pylori-associated gastrointestinal diseases. Carriers of «antigenic» blood groups A (II), B (III), AB (IV) are more susceptible to development of infectious, cardiovascular and cancer diseases. The presented data demonstrate clinical significance of the definition of group typing not only for selection of blood and its components during transfusion and transplantation, but also for diagnostics, determination of risk group and tactics for treatment patients with different nosologies.


1979 ◽  
Vol 149 (4) ◽  
pp. 975-980 ◽  
Author(s):  
T Feizi ◽  
R A Childs ◽  
K Watanabe ◽  
S I Hakomori

Blood group I activities of the purified glycosphingolipid lacto-N-iso-octaosyl ceramide (Fromula: see text) and 8 of its analogues have been evaluated with 11 anti-I sera including 5 anti-I sera previously tested. All but one of the antisera were inhibited by the lacto-N-iso-octaosyl structure. Three types of I-specificity could be distinguished although none of the anti-I sera was identical in its inhibition patterns with the nine glycophingolipid analogues. The anti-I sera Ma and Woj represent the first type and require an intact Galbeta1 leads to 4GlcNAcbeta1 leads to 6 chain, the anti-I sera Step, Gra, Ver, and Ful represent the second type which requires Galbeta1 leads to 4GlcNAcbeta1 leads to 3 chain with branching, and the anti-I sera Phi, Da, Sch, and Low belong to the third type which requires both branches to be intact. Anti-I antibodies varry in their ability to react with their antigenic determinants in the presence of external substitutions with alpha-linked galactose or sialic acid.


1983 ◽  
Vol 59 (1) ◽  
pp. 245-256
Author(s):  
J.P. McCoy ◽  
D. Schrier ◽  
E.J. Lovett ◽  
W.J. Judd ◽  
J. Varani

Commercially prepared ABO blood-typing antisera have been tested for their ability to bind to murine laminin and their cytotoxic effects upon high and low metastatic variants of a murine fibrosarcoma. Previous studies have shown that alpha-D-galactopyranosyl end-groups comprise the major antigenic determinants on type B erythrocytes and that these same end-groups are present on murine laminin purified from the EHS sarcoma and on a laminin-like glycoprotein on the surface of the high, but not low, metastatic fibrosarcoma cells. In the present study we found that all sera containing anti-B activity were cytotoxic to the high, but not the low, metastatic cells and that all of these sera reacted strongly against immobilized murine laminin in an enzyme-linked immunosorbent assay. Sera lacking anti-B activity, i.e. anti-A antisera, were much less cytotoxic to either cell line and three of the four anti-A sera did not bind to murine laminin. The laminin reactivity and cytotoxic effect of the anti-B sera were specifically abrogated by preincubation of the sera with water-soluble blood group B substance or with murine laminin but not with water-soluble blood group A substance.


1966 ◽  
Vol 123 (6) ◽  
pp. 1061-1081 ◽  
Author(s):  
Manuel E. Kaplan ◽  
Elvin A. Kabat

Insoluble blood group substances prepared by copolymerization of soluble blood group substances with N-carboxy-L-leucine anhydride were used to absorb blood group antibodies from two human, high-titered anti-A sera. After the absorbants were washed free of nonspecific serum proteins, blood group antibodies were eluted either with pH 3.62 acetate buffer, or at neutral pH with monosaccharide haptens of the A or B antigenic determinants (N-acetyl-D-galactosamine or D-galactose respectively). The purified anti-A antibodies were characterized, immunoelectrophoretically, as γM-, γA-, and γG-immunoglobulins. These were further separated into γM- and γG-fractions by gel filtration or density gradient centrifugation. Both γM- and one of the two γG-antibody fractions contained K and L light chain determinants; the remaining γG-fraction was comprised, almost totally, of type K molecules. Precipitability of the purified anti-A immunoglobulins by blood group A substance varied from 43 to 89%. The agglutinating activity per unit N of the isolated γG-anti-A was found to equal, in one case, and to exceed, in the second, that of the γM-antibodies from the same individuals. The marked differences between γM- and γG-antibody fractions in quantitative hapten inhibition studies were interpreted to mean that the antibody-combining site of the isolated eluted γG-anti-A was significantly larger than that of the eluted γM-anti-A. Whether these data connote differences in combining site size between entire immunoglobulin classes in an individual serum or simply reflect the properties of highly selected antibody populations cannot be stated at present.


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