Low-molecular-weight Ia antigens in normal mouse serum

1976 ◽  
Vol 3 (1) ◽  
pp. 455-463 ◽  
Author(s):  
Christopher R. Parish ◽  
David C. Jackson ◽  
Ian F. C. McKenzie
1976 ◽  
Vol 3 (1) ◽  
pp. 129-137 ◽  
Author(s):  
Christopher R. Parish ◽  
Aira B. Chilcott ◽  
Ian F. C. McKenzie

1976 ◽  
Vol 3 (1) ◽  
pp. 113-128 ◽  
Author(s):  
Christopher R. Parish ◽  
Aira B. Chilcott ◽  
Ian F. C. McKenzie

1977 ◽  
Vol 145 (4) ◽  
pp. 1039-1053 ◽  
Author(s):  
I F McKenzie ◽  
A Clarke ◽  
C R Parish

We have previously reported that the Ia specificities, coded for by the I region within the H-2 complex, appear to consist predominantly of carbohydrate. This conclusion was reached by examining low molecular weight Ia-bearing oligosacharides isolated from mouse serum. We now report hapten-inhibition studies which indicate that the binding of both allogeneic and xenogeneic anti-Ia antibodies to the Ia glycoproteins found predominantly on B lymphocytes can be specifically inhibited by certain free sugars. Both inhibition assays revealed that the specificity for the following Ia antigens resides predominantly in the following sugars: (a) Ia.1: N-acetyl-D-mannosamine or related sugars; (b) Ia.3: alpha-D-galactose and related sugars; (c) Ia.7: L-fucose; and (d) Ia.15: N-acetyl-D-glucosamine. It seems likely that these sugars are found at the terminal nonreducing ends of the carbohydrate portion of the Ia-bearing glycoproteins present in the lymphocyte membrane. In contrast, several public and private H-2 antigenic specificities did not appear to be sugar defined. These studies imply that at least some of the Ia genes from both the I-A and I-C subregions of the I region code for glycosyl transferases which modify oligosaccharide structure and impart specificity to the Ia antigens by alteration of their terminal sugar residues.


Virology ◽  
1979 ◽  
Vol 98 (1) ◽  
pp. 20-34 ◽  
Author(s):  
Ronald C. Montelaro ◽  
Peter J. Fischinger ◽  
Susan B. Larrick ◽  
Nancy M. Dunlop ◽  
James N. Ihle ◽  
...  

2009 ◽  
Vol 49 (1) ◽  
pp. 36-45 ◽  
Author(s):  
Christer Lindqvist ◽  
Carol Dahl ◽  
Carita Back ◽  
Christian Oker-Blom ◽  
Karl Akerman ◽  
...  

1974 ◽  
Vol 20 (4) ◽  
pp. 535-544 ◽  
Author(s):  
K. B. Orr ◽  
F. Paraskevas

Serum collected from BALB/c mice 6 h after the intraperitoneal injection of Freund's complete adjuvant when mixed with a soluble antigen such as bovine serum albumin or human fibrinogen forms a cytophilic Ig which is taken up by the normal mouse spleen cells. When the serum was absorbed with an aggregated form of antigen, subsequent addition of soluble antigen failed to induce formation of cytophilic Ig, but an eluate recovered from the aggregated antigen did.This property of the serum is most likely non-specific since any antigen thus far tested is effective in inducing formation of cytophilic Ig and furthermore, absorption with one kind of antigen abolished the ability of the serum to form cytophilic Ig upon subsequent addition of any other antigen. Upon fractionation of the serum on Sephadex G-200 the activity was recovered in the 7-S fraction. However, the 4-S fraction (which lacks Ig) contained a factor which in the presence of antigen and normal mouse serum or its 7-S fraction formed a cytophilic Ig. The existing evidence indicated that the cytophilic Ig was taken up by 25 to 35% of the T cells (θ positive). Furthermore, about 15% of Ig carrying cells also took up the cytophilic Ig.The cytophilic Ig belongs to the IgG (IgG2a) class and presumptive evidence suggested that it may represent a complex of Ig and antigen.


1980 ◽  
Vol 130 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Curtis L. Parker ◽  
Douglas F. Paulsen ◽  
Joseph A. Rosebrock ◽  
W.Craig Hooper

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