Development of human ABO blood group A antigen on <i>Escherichia coli</i> Y1089 and Y1090

Yang, Nan; Boettcher, B.

doi:10.1038/icb.1992.54

Cited by 5 publications

(2 citation statements)

References 6 publications

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“…Bacteria could be an important target for such an Ab (eg, see Muschel 35 ). Indeed, the presence of carbohydrate substances on bacteria 36,37 or other antigenic carriers entering the gut is after all the main suspected reason for the initial development in neonates of ABO Ab, as well as Ab against Gal␣1-3Gal. 19,20 In addition, severe viral diseases have been implicated in this regard (eg, small pox).…”

Section: Discussionmentioning

confidence: 99%

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement

Preece

Strahan

Devitt

et al. 2002

Blood

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No definitive biologic function has been associated with the human ABO histoblood group polymorphism, or any other terminal carbohydrate differences within or between closely related species. We have experimentally addressed the question of whether viral particles can become glycosylated as determined by the glycosylation (eg, ABO) status of the producer cell and as a result be affected by human serum containing specific natural antibodies (NAbs). Measles virus was produced in cells transfected with cDNA encoding, either human A-transferase, B-transferase, an inactive "O-transferase," or a pig ␣1-3galactosyltransferase (␣1-3GT) synthesizing the Gal␣1-3Gal structure. The viruses were shown to carry the same ABO structures as the cells; that is, A but not B if produced in A-type cells, and B but not A if produced in B-type cells. Only O was detected on the virus produced from O-type cells, whereas reduced amounts of O appeared on the Aand B-type viral particles. In addition, the Gal␣1-3Gal structure was transferred onto measles only when grown in human cells expressing this structure. When subjected to human preimmune sera, the A-type, the B-type, and the Gal␣1-3Gal viral particles were partially neutralized in a complement-dependent manner. However, the O-type or the Gal␣1-3Gal-negative viral particles were not neutralized. The neutralization appeared to be mediated by specific NAb, as judged by specific inhibition using synthetic A and IntroductionThe ABO (or ABH) histo-blood group system is characterized by the expression of polymorphic carbohydrate termini on several cell types. The genetic basis for this polymorphism in humans is explained by the existence of allelic forms of a single gene encoding glycosyltransferases with specificity for different monosaccharides. 1 They appear to be evolutionarily old, being present on glycosylated structures in different eukaryotic as well as prokaryotic organisms, and established their present day polymorphic form in humans at the latest during early primate evolution (for a review, see Blancher et al 2 ). Hence, it would be surprising if the ABO structures did not serve an important purpose. No definitive biologic function has, however, as yet been identified, 3 although suggestions have often centered on immunologic explanations. [4][5][6][7] Another very similar terminal carbohydrate structure, the Gal␣1-3Gal␤1-4GlcNAc-R (referred to as Gal␣1-3Gal) is present in other mammals but not in humans and other Old World primates. 8 Bacteria mimicking vertebrate terminal carbohydrates may have given rise to selection pressures favoring polymorphic glycans. 9 In addition, many pathogens and their toxins bind to specific terminal carbohydrate structures and may consequently produce selection pressures affecting the evolution of terminal carbohydrate structures. 7,10 It has also been previously suggested that viruses may carry ABO structures as part of their envelope 11,12 and consequently serve as potential selective forces influencing ABO genotype frequencies in a population....

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Section: Discussionmentioning

confidence: 99%

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement

Preece

Strahan

Devitt

et al. 2002

Blood

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“…Therefore, it is conceivable that the cross-reactive antibody response is maintained as the result of cross-recognition to host antigens. Additionally, it may be postulated that the antibody response is chronically stimulated due to exposure to enteric commensal organisms in a manner similar to the immune response maintained against blood group antigens (Drach et al 1972, Yang andBoettcher 1992).…”

Section: Discussionmentioning

confidence: 99%

Induction of myosin cross-reactive antibody and cytolytic T cell responses in mice with Streptococcus pyogenes

Cunningham¹

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Induction of Myosin Cross-Reactive Antibody and Cytolytic T Cell Responses in mice with Streptococcus pyogenes Cynthia Cunningham Impetigo and pharyngitis are two common suppurative infections in man elicited by Streptococcus pyogenes that lead to autoimmune complications in susceptible individuals. Although the underlying mechanisms for the onset of post-streptococcal autoimmunity have yet to be established, experimental information gained thus far suggests that the resultant pathology is a consequence of immunological cross-reactivity between streptococcal antigens, namely the anti-phagocytic factor M protein and host proteins, specifically myosin. Experimental animal model systems developed to date have predominantly relied on the immunization of adult animals with M protein emulsed in adjuvant. In the laboratory we have undertaken studies with mice to examine the capacity of S. pyogenes as whole organism without adjuvant to elicit autoreactive B and T lymphocytes. We have observed that immunizing mice with heat-killed preparations of S. pyogenes as neonates, but not adults, induces the production of host cross-reactive serum antibodies akin to those documented in cases of post-streptococcal autoimmunity. Western blot analysis of monoclonal antibodies generated from mice immunized with S. pyogenes suggests that antibodies induced in neonatal mice preferentially recognize the cardiac isoforms of mouse skeletal myosin, whereas, antibodies derived from adult mice primarily recognize determinants shared by all isoforms of mouse skeletal myosin. In addition, we have demonstrated the ability of neonatal, but not adult, mice to mount a myosin-reactive CD8 + cytotoxic T cell response following immunization with S. pyogenes. Our observations indicate that the response is additionally dependent on the genetic background of mice, the route of immunization, and requires M protein. In summation, our results suggest that in susceptible individuals exposure to S. pyogenes early in life may serve as a priming event and following a subsequent event later in life, possibly re-exposure to S. pyogenes, allow the initiation of the pathology associated with poststreptococcal autoimmunity. These results contribute to the understanding of the development of the mechanisms of post-streptococcal autoimmune complications and may ultimately contribute to the development of effective diagnostic intervention strategies. iii Dedication I dedicate this dissertation to my parents, James and Judith McDaniel, whose example and uncompromising devotion and support have given me the courage to accept challenges and the strength to accomplish my goals.

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Gene usage for naturally occurring antibodies

Nydegger¹,

Moerenhout²,

Tinguely³

et al. 2001

Transplantation Proceedings

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Development of human ABO blood group A antigen on Escherichia coli Y1089 and Y1090

Cited by 5 publications

References 6 publications

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement

Induction of myosin cross-reactive antibody and cytolytic T cell responses in mice with Streptococcus pyogenes

Gene usage for naturally occurring antibodies

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