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Glycoconjugate journal2006; 23(7-8); 585-590; doi: 10.1007/s10719-006-8188-8

Presence of natural anti-Galalpha1-4GalNAcbeta1-3Gal (anti-NOR) antibodies in animal sera.

Abstract: Rare polyagglutinable NOR erythrocytes contain unusual globoside extention products terminating with a Galalpha1-4GalNAcbeta1-3Gal- unit. This trisaccharide epitope is recognized by recently characterized antibodies naturally occurring in most human sera (Duk et al., Glycobiology, 15, 109, 2005). These antibodies represent two major types of fine specificity. All these antibodies are most strongly inhibited by Galalpha1-4GalNAcbeta1-3Gal (NOR-tri), and weakly by Galalpha1-4Gal. However, the type 1 antibodies are strongly inhibited by Galalpha1-4Galbeta1-3Gal-R and weakly by Galalpha1-4GalNAc, while the type 2 antibodies show the opposite reactivities with these two oligosaccharides. Similar antibodies have now been found in horse, rabbit and pig sera. The antibodies were purified from animal sera by affinity chromatography on Galalpha1-4GalNAcbeta1-3Gal-human serum albumin(HSA)-Sepharose 4B conjugate. The specificity of the antibodies was determined by binding to ELISA plates coated with several alpha-galactosylated oligosaccharide-polyacrylamide (PAA) or -HSA conjugates and by inhibition with synthetic oligosaccharides. The purified antibodies bound specifically to conjugates containing NOR-tri. The inhibition of binding showed that the animal sera also contain two types of anti-NOR antibodies: type 2 was found in the horse serum, and a mixture of both types was present in rabbit and pig serum. These results indicate that anti-NOR, a new and distinct kind of anti-alphaGal antibody, are present in animal sera and show similar specificties and diversity as their counterparts found in human sera.
Publication Date: 2006-09-29 PubMed ID: 17006649DOI: 10.1007/s10719-006-8188-8Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This study investigates the presence of anti-Galalpha1-4GalNAcbeta1-3Gal (anti-NOR) antibodies in animal blood, which have previously been found in most human blood samples. The findings suggest that these specific antibodies also exist in animal blood, with similar characteristics as those in human blood.

Understanding Anti-NOR Antibodies

This research is centered around the study of anti-Galalpha1-4GalNAcbeta1-3Gal (anti-NOR) antibodies. These antibodies interact with a specific trisaccharide epitope found on NOR erythrocytes, a rare type of red blood cell. This specific interaction was only recently discovered and found to naturally occur in most human blood samples.

  • Type 1 antibodies are inhibited strongly by Galalpha1-4Galbeta1-3Gal-R and weakly by Galalpha1-4GalNAc.
  • Type 2 antibodies display the opposite reaction, being weakly inhibited by Galalpha1-4Galbeta1-3Gal-R and strongly by Galalpha1-4GalNAc.

Presence of Anti-NOR Antibodies in Animals

This paper reveals that anti-NOR antibodies are not exclusive to humans; they are also found in horse, rabbit, and pig blood. These animal’s sera samples were tested for these antibodies using a technique known as affinity chromatography.

  • Using this technique, the research found that horse serum contained type 2 anti-NOR antibodies.
  • Rabbit and pig serum presented a mixture of both type 1 and type 2 antibodies.

Research Implications and Conclusions

The detection of these antibodies in various animal sera indicates that anti-NOR antibodies are not unique to human sera. Moreover, the antibody types and their respective inhibitions seem to be conserved across the different species. These antibodies, figuring under a new and distinct category of anti-alphaGal antibodies, could potentially broaden our understanding of immune responses across species. Further research is required to determine the precise role and impact of these antibodies on animal health and disease.

Cite This Article

APA
Duk M, Lisowska E. (2006). Presence of natural anti-Galalpha1-4GalNAcbeta1-3Gal (anti-NOR) antibodies in animal sera. Glycoconj J, 23(7-8), 585-590. https://doi.org/10.1007/s10719-006-8188-8

Publication

ISSN: 0282-0080
NlmUniqueID: 8603310
Country: United States
Language: English
Volume: 23
Issue: 7-8
Pages: 585-590

Researcher Affiliations

Duk, Maria
  • Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Rudolf Weigl St. 12, 53-114, Wroclaw, Poland.
Lisowska, Elwira

    MeSH Terms

    • ABO Blood-Group System / immunology
    • Animals
    • Antibodies / blood
    • Antibody Specificity
    • Erythrocytes / immunology
    • Globosides / immunology
    • Horses
    • Humans
    • Immunity, Innate
    • Oligosaccharides / pharmacology
    • Rabbits
    • Species Specificity
    • Sus scrofa
    • Trisaccharides / immunology

    References

    This article includes 14 references
    1. Duk M, Reinhold BB, Reinhold VN, Kusnierz-Alejska G, Lisowska E. Structure of a neutral glycosphingolipid recognized by human antibodies in polyagglutinable erythrocytes from the rare NOR phenotype.. J Biol Chem 2001 Nov 2;276(44):40574-82.
      pubmed: 11504714doi: 10.1074/jbc.M102711200google scholar: lookup
    2. Perepelov AV, Ujazda E, Senchenkova SN, Shashkov AS, Kaca W, Knirel YA. Structural and serological studies on the O-antigen of Proteus mirabilis O14, a new polysaccharide containing 2-[(R)-1-carboxyethylamino]ethyl phosphate.. Eur J Biochem 1999 Apr;261(2):347-53.
    3. Korchagina EY, Pochechueva TV, Obukhova PS, Formanovsky AA, Imberty A, Rieben R, Bovin NV. Design of the blood group AB glycotope.. Glycoconj J 2005 Mar;22(3):127-33.
      pubmed: 16133833doi: 10.1007/s10719-005-0508-xgoogle scholar: lookup
    4. Westerlind U, Hagback P, Duk M, Norberg T. Synthesis and inhibitory activity of a di- and a trisaccharide corresponding to an erythrocyte glycolipid responsible for the nor polyagglutination.. Carbohydr Res 2002 Sep 27;337(17):1517-22.
      pubmed: 12350319doi: 10.1016/s0008-6215(02)00222-7google scholar: lookup
    5. Kuśnierz-Alejska G, Duk M, Storry JR, Reid ME, Wiecek B, Seyfried H, Lisowska E. NOR polyagglutination and Sta glycophorin in one family: relation of NOR polyagglutination to terminal alpha-galactose residues and abnormal glycolipids.. Transfusion 1999 Jan;39(1):32-8.
    6. Mourad R, Morelle W, Neveu A, Strecker G. Diversity of O-linked glycosylation patterns between species. Characterization of 25 carbohydrate chains from oviducal mucins of Rana ridibunda.. Eur J Biochem 2001 Apr;268(7):1990-2003.
    7. Galili U. Immune response, accommodation, and tolerance to transplantation carbohydrate antigens.. Transplantation 2004 Oct 27;78(8):1093-8.
    8. Parker W, Lateef J, Everett ML, Platt JL. Specificity of xenoreactive anti-Gal alpha 1-3Gal IgM for alpha-galactosyl ligands.. Glycobiology 1996 Jul;6(5):499-506.
      pubmed: 8877370doi: 10.1093/glycob/6.5.499google scholar: lookup
    9. Vinogradov EV, Kaca W, Knirel YA, Rózalski A, Kochetkov NK. Structural studies on the fucosamine-containing O-specific polysaccharide of Proteus vulgaris O19.. Eur J Biochem 1989 Mar 1;180(1):95-9.
    10. Parker W, Lin SS, Yu PB, Sood A, Nakamura YC, Song A, Everett ML, Platt JL. Naturally occurring anti-alpha-galactosyl antibodies: relationship to xenoreactive anti-alpha-galactosyl antibodies.. Glycobiology 1999 Sep;9(9):865-73.
      pubmed: 10460828doi: 10.1093/glycob/9.9.865google scholar: lookup
    11. Harris PA, Roman GK, Moulds JJ, Bird GW, Shah NG. An inherited RBC characteristic, NOR, resulting in erythrocyte polyagglutination.. Vox Sang 1982 Mar;42(3):134-40.
    12. Duk M, Westerlind U, Norberg T, Pazynina G, Bovin NN, Lisowska E. Specificity of human anti-NOR antibodies, a distinct species of "natural" anti-alpha-galactosyl antibodies.. Glycobiology 2003 Apr;13(4):279-84.
      pubmed: 12626386doi: 10.1093/glycob/cwg036google scholar: lookup
    13. Duk M, Kusnierz-Alejska G, Korchagina EY, Bovin NV, Bochenek S, Lisowska E. Anti-alpha-galactosyl antibodies recognizing epitopes terminating with alpha1,4-linked galactose: human natural and mouse monoclonal anti-NOR and anti-P1 antibodies.. Glycobiology 2005 Feb;15(2):109-18.
      pubmed: 15342552doi: 10.1093/glycob/cwh146google scholar: lookup
    14. Lisowska E, Duk M. Polyagglutination NOR: new glycosphingolipid antigens recognized by a new type of common human anti-alpha-galactosyl antibodies.. Arch Biochem Biophys 2004 Jun 15;426(2):142-7.
      pubmed: 15158664doi: 10.1016/j.abb.2004.02.035google scholar: lookup

    Citations

    This article has been cited 2 times.
    1. Doherty MK, Shaw C, Woods L, Weimer BC. Alpha-Gal Bound Aptamer and Vancomycin Synergistically Reduce Staphylococcus aureus Infection In Vivo. Microorganisms 2023 Jul 8;11(7).
    2. Bereznicka A, Mikolajczyk K, Szymczak-Kulus K, Kapczynska K, Majorczyk E, Modlinska A, Piasecki T, Kaczmarek R, Czerwinski M. Two Paralogous Gb3/CD77 Synthases in Birds Show Different Preferences for Their Glycoprotein and Glycosphingolipid Substrates. Int J Mol Sci 2021 Sep 9;22(18).
      doi: 10.3390/ijms22189761pubmed: 34575935google scholar: lookup