Literature DB >> 6155326

Characterization of the T antigen and T agglutinin in inbred rats.

S A Noeman, D N Misra, T J Gill.   

Abstract

Treatment of rat erythrocytes with vibrio cholerae neuraminidase (VCN) exposed antigenic determinants on the cell surface membrane, and autologous rat serum contained antibodies which reacted with these determinants and with VCN-treated human erythrocytes. The antibodies were not present in sera of animals less than 8 weeks of age. Human serum also contained antibodies which reacted with the VCN-treated rat erythrocytes. Lectin isolated and purified from Arachis hypogoea agglutinated VCN-treated rat erythrocytes. This system has the characteristics of the T antigen which had been described initially in humans. Absorption studies showed that the VCN-treated rat erythrocyte membrane antigen cross-reacted with the VCN-treated human erythrocyte membrane antigen. Absorption of rat sera and the lectin solution with VCN-treated rat or human erythrocytes removed all of the molecules capable of reacting with both rat and human erythrocytes. Absorption of human sera with VCN-treated human cells removed their reactivity with both cell types, but absorption with VCN-treated rat cells did not remove completely their reactivity with VCN-treated human erythrocytes. These results indicate that the VCN-treated rat cells contain antigenic determinants which are identical to some on the VCN-treated human cells and that the human sera contain antibodies to additional antigenic specificities not shared with rat red blood cells. Haemagglutination inhibition studies with different sugars, T antigen from human erythrocyte membranes and desialylated glycoprotein from rat erythrocyte membranes showed that the T antigen, the desialylated glycoprotein and the sugars containing a terminal non-reducing beta-D-galactosyl residue inhibited the reactivity of the lectin, the rat sera and the human sera with both human and rat red blood cells. These findings show that the antigenic reactivity of the VCN-treated rat red blood cells residues in the membrane glycoproteins and that the immunodominant group is a carbohydrate. Thus, the rat has a T antigenic system very similar to that of the human.

Entities:  

Mesh:

Substances:

Year:  1980        PMID: 6155326      PMCID: PMC1457953     

Source DB:  PubMed          Journal:  Immunology        ISSN: 0019-2805            Impact factor:   7.397


  20 in total

1.  Purification and characterization of a hemagglutinin from Arachis hypogeae.

Authors:  T Terao; T Irimura; T Osawa
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1975-11

2.  Chemical studies of erythrocyte membrane glycoproteins from several species.

Authors:  B G Hudson; L J Wegener; J M Wingate; K L Carraway
Journal:  Comp Biochem Physiol B       Date:  1975-05-15

3.  Solubilization and comparative analysis of mammalian erythrocyte membrane glycoproteins.

Authors:  H Hamaguchi; H Cleve
Journal:  Biochem Biophys Res Commun       Date:  1972-04-28       Impact factor: 3.575

4.  On the specificity of lectins with a broad agglutination spectrum. II. Studies on the nature of the T-antigen and the specific receptors for the lectin of Arachis hypogoea (ground-nut).

Authors:  G Uhlenbruck; G I Pardoe; G W Bird
Journal:  Z Immunitatsforsch Allerg Klin Immunol       Date:  1969-11

5.  Studies on the nature of the T-antigen and the problem of panagglutination.

Authors:  Z Kim; G Uhlenbruck; G I Pardoe
Journal:  Nihon Hoigaku Zasshi       Date:  1970-05

6.  An agglutinin from Helix pomatia, which reacts with terminal N-acetyl-D-galactosamine.

Authors:  G Uhlenbruck; O Prokop
Journal:  Vox Sang       Date:  1966 Jul-Aug       Impact factor: 2.144

7.  Further characterization of some heterophile agglutinins reacting with alkali-labile carbohydrate chains of human erythrocyte glycoproteins.

Authors:  W Dahr; G Uhlenbruck; G W Bird
Journal:  Vox Sang       Date:  1975       Impact factor: 2.144

8.  Peanut agglutinin, a new mitogen that binds to galactosyl sites exposed after neuraminidase treatment.

Authors:  A Novogrodsky; R Lotan; A Ravid; N Sharon
Journal:  J Immunol       Date:  1975-11       Impact factor: 5.422

9.  The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea).

Authors:  R Lotan; E Skutelsky; D Danon; N Sharon
Journal:  J Biol Chem       Date:  1975-11-10       Impact factor: 5.157

10.  Immunofluorescent studies on antibodies directed to a buried membrane structure present in lymphocytes and erythrocytes.

Authors:  R J Winchester; S M Fu; J B Winfield; H G Kunkel
Journal:  J Immunol       Date:  1975-01       Impact factor: 5.422

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.