Structural comparison of glycophorins and immunochemical analysis of genetic variants

Furthmayr, Heinz

doi:10.1038/271519a0

Cited by 286 publications

(85 citation statements)

References 37 publications

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“…It is still possible, however, that glycophorin B, which has a sequence identical to the N form of glycophorin A for at least the first 23 N-terminal amino acids (Furthmayr, 1978), may also be involved in influenza C virus binding. Treatment of M(+) N(-) erythrocytes with anti-N antibody inhibited virus attachment by about 20 ~o while anti-M treatment of M( -) N(+) cells did not inhibit at all (see Table 4), raising the possibility that part of the receptor activity of human erythrocytes might be associated with glycophorin B.…”

Section: Discussionmentioning

confidence: 99%

Attachment of Influenza C Virus to Human Erythrocytes

Nishimura

Sugawara²,

Kitame³

et al. 1988

Journal of General Virology

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SUMMARYBinding experiments with radioactively labelled influenza C virions were carried out to investigate the interaction of the virus with human erythrocytes. The erythrocytes from any of 35 different individuals were found to contain influenza C virus-binding sites though their number was variable among the individuals and was much less than that on mouse, rat and chicken erythrocytes. Attachment of influenza C virus to human erythrocytes was inhibited completely by prior treatment of the virus with anti-HE monoclonal antibody having a strong haemagglutination inhibition activity. Pretreatment of erythrocytes with neuraminidase or the neuraminate-O-acetylesterase of influenza C virus resulted in a marked reduction in the level of virus binding. Thus it appears that human erythrocytes have a low level of O-acetylated sialic acid-containing glycoconjugates that can interact specifically with the HE glycoprotein of influenza C virus. Proteolytic digestion of erythrocytes with ficin, bromelain or V-8 protease inhibited virus binding almost completely, suggesting that the erythrocyte receptor for influenza C virus is a glycoprotein. In contrast to these enzymes, trypsin treatment of erythrocytes reduced virus binding by only about 50~, and ~-chymotrypsin treatment did not inhibit at all. It was also found that treatment of erythrocytes with monoclonal antibody to the M or N blood group antigen greatly inhibited virus binding to the cells. These results, taken together, suggest that most influenza C virus receptors on human erythrocytes, if not all, reside on glycophorin A which is known to possess the M or N blood group activity.

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Section: Discussionmentioning

confidence: 99%

Attachment of Influenza C Virus to Human Erythrocytes

Nishimura

Sugawara²,

Kitame³

et al. 1988

Journal of General Virology

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“…Thus, each of these Tn mAbs, in addition to requiring GalNAc, also requires a specific peptide determinant on GPA or GPB. Neuraminidase cleaves the two N-acetylneuraminic acid residues present on the NeuNAca2-3Gal pl-3 (NeuNAca2-6)GalNAcul-0-Ser (Thr) tetrasaccharides present a t 15 sites on GPA and 11 sites on the 35 amino acid N-terminal portion of GPB [17,21,36,46,54]. Since the Tn mAbs do not bind to fixed normal or neuraminidase-digested erythrocytes, they will not recognize the GPAiGPB binding sites when GalNAc is in the normal tetrasaccharide or in the form of Galp1-3GalNAcal-O-Ser(Thr) disaccharide.…”

Section: Discussionmentioning

confidence: 99%

Flow cytometric analysis of erythrocyte populations in tn syndrome blood using monoclonal antibodies to glycophorin A and the Tn antigen

et al. 1990

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Flow cytometric analysis employing monoclonal antibodies to the Tn antigen and glycophorin A was used to characterize the erythrocyte populations present in blood samples from individuals with Tn syndrome. Four monoclonal antibodies specific for the Tn antigen, GalNAc monosaccharide, on human erythrocytes were obtained from a fusion of splenocytes from a Biozzi mouse immunized with red cells from a Tn individual. These monoclonal antibodies specifically recognize GalNAc monosaccharide sites located on the erythrocyte cell surface sialoglycoproteins, glycophorin A and glycophorin B, and do not bind to fixed normal red cells presenting the Neu‐NAcα2‐3Galβ1‐3(NeuNAcα2‐6)GalNAcα1‐O‐Ser(Thr) tetrasaccharide or to fixed neuraminidase‐digested cells presenting the Gal‐GalNAc disaccharide. The percentages of Tn‐positive red cells in samples from six unrelated Tn donors ranged from 28 to 99%. Binding of the glycophorin A‐specific monoclonal antibodies showed that the erythrocytes composing the Tn‐negative fraction presented normal amounts of the M and N epitopes on glycophorin A. The presumed somatic mutational origin of Tn‐positive cells was tested in blood samples from five normal donors; three possible Tn cells were observed after analysis of a total of 1.1 X 107 erythrocytes, suggesting that the frequency of such cells in normal individuals is > 1 X 10−6.

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“…It contains an intramembraneous hydrophobic amino acid sequence which evidently interacts with membrane lipids. Normal cells contain ~106 copies of glycophorin A/cell [15], whereas En(a-) red cells completely lack the protein [9,16]. The availability of this naturally occurring red cell variant gives an excellent possibility to study the influence of glycophorin A on the structure and function of red cell membranes.…”

Section: Discussionmentioning

confidence: 99%