scholarly journals SfaNl Polymorphism Distinguishes the Alleles of the Glycophorin A Locus That Determine the MN Blood Group

1997 ◽  
Vol 98 (1) ◽  
pp. 51-53 ◽  
Author(s):  
Sharon H. Leos ◽  
William L. Bigbee ◽  
Ronald H. Jensen ◽  
Stephen G. Grant
Keyword(s):  
Blood Group ◽  
Glycophorin A ◽  
Mn Blood Group

scholarly journals Systematic classification of alleles of the glycophorin A (MN blood group) gene

2005 ◽  
Vol 50 (12) ◽  
pp. 667-670
Author(s):  
Hajime Mizukami ◽  
Atsushi Akane ◽  
Nori Nakayashiki ◽  
Yasuhiro Aoki ◽  
Hiroshi Shiono
Keyword(s):  
Blood Group ◽  
Glycophorin A ◽  
Systematic Classification ◽  
Mn Blood Group

scholarly journals The role of sialic acid in the expression of human MN blood group antigens.

1979 ◽  
Vol 254 (6) ◽  
pp. 2112-2119 ◽  
Author(s):  
J.E. Sadler ◽  
J.C. Paulson ◽  
R.L. Hill
Keyword(s):  
Sialic Acid ◽  
Blood Group ◽  
Blood Group Antigens ◽  
Mn Blood Group

Primate genes for glycophorins carrying MN blood group antigens

1993 ◽  
Vol 22 (1) ◽  
pp. 7-12
Author(s):  
Shinichi Kudo ◽  
Masaaki Onda ◽  
Ann Rearden ◽  
Minoru Fukuda
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Mn Blood Group

Anti-Tm, an Antibody Defining a New Antigenic Determinant within the MN Blood-Group System

Vox Sanguinis ◽  
1965 ◽  
Vol 10 (6) ◽  
pp. 742-743
Author(s):  
P.D. Issitt ◽  
Jane M. Haber ◽  
F.H. Allen jr.
Keyword(s):  
Blood Group ◽  
Antigenic Determinant ◽  
Blood Group System ◽  
Group System ◽  
Mn Blood Group

HLA-restricted lymphoproliferative responses to MN blood group determinants

Nature ◽  
1982 ◽  
Vol 299 (5878) ◽  
pp. 67-69 ◽  
Author(s):  
M. A. Blajchman ◽  
N. Heddle ◽  
N. Naipul ◽  
D. P. Singal
Keyword(s):  
Blood Group ◽  
Mn Blood Group

scholarly journals Anti-M monoclonal antibodies cross-reacting with variant Mg antigen: an example of modulation of antigenic properties of peptide by its glycosylation

Blood ◽  
1994 ◽  
Vol 84 (7) ◽  
pp. 2340-2345 ◽  
Author(s):  
E Jaskiewicz ◽  
M Czerwinski ◽  
D Syper ◽  
E Lisowska
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Blood Group ◽  
Polypeptide Chain ◽  
Protein Glycosylation ◽  
Glycophorin A ◽  
Amino Acid Residues ◽  
Terminal Portion ◽  
Peptide Analogs ◽  
Antigenic Properties

Abstract Some monoclonal antibodies (MoAbs) directed against blood group M- related epitope of glycophorin A (GPA) were found to agglutinate rare variant erythrocytes carrying GPA of Mg type. In contradistinction to normal GPA-M or -N, the N-terminal portion of GPA-Mg is not glycosylated. Therefore, the multipin peptide synthesis was used for testing the specificity of the cross-reacting MoAbs. Among several anti- M and anti-N MoAbs tested, only three anti-M (E3, E6, 425/2B) agglutinated Mg erythrocytes and showed binding to the synthetic octapeptides corresponding to N-terminal sequences of GPA-M (SSTTGVAM), GPA-N (LSTTEVAM), and GPA-Mg (LSTNEVAM). Testing multiple peptide analogs (window and replacement analysis) showed that these MoAbs were specific for peptidic epitope in which Met8 and Val6 were the most essential amino acid residues. The amino acid replacements Ser<-->Leu1 or Gly<-->Glu5 (M v N) and Thr<-->Asn4 (M and N v Mg) had no or negligible effect on the reaction of synthetic peptides with the MoAbs. However, when Ser2, Thr3, and Thr4 carry O-linked sialooligosaccharides (normal GPA-M or -N), the MoAbs recognize Gly5- and sialic acid- dependent blood group M-related epitope. An interesting finding concerning anti-M/Mg MoAbs described here is the fact that glycosylation of amino acid residues adjacent to the most important part of peptidic epitope not only differentially modulates the proper exposure of peptidic epitope, but also alters the requirement for some amino acid residues present within the epitope. Pathologic conditions, including hematologic disorders, are often accompanied by alterations in protein glycosylation, resulting not only from differences in the structure of antigen polypeptide chain, but also from changes in specificity or expression of enzymes involved in glycosylation. Our present findings draw attention to possibility of the bidirectional modulation of protein antigenicity by glycosylation and may be helpful in interpretation of some results obtained with MoAb used for diagnostic or other purposes.

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