Skip to main content
PMC home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1969 Apr;48(4):664–673. doi: 10.1172/JCI106024

Ecological studies of intestinal bacteria. Relation between the specificity of fecal ABO blood group antigen-degrading enzymes from enteric bacteria and the ABO blood group of the human host

Lansing C Hoskins 1
PMCID: PMC322271  PMID: 5774105

Abstract

This report presents evidence for enteric bacterial adaptation to genetically controlled environmental factors in the individual human host. Human feces contains bacterial enzymes that degrade water-soluble A, B, and H antigens, and both the presence and the specificity of ABH blood group antigens in human gut mucous secretions are genetically determined for each individual. In this study, partially purified fecal blood group antigen-degrading enzymes from 31 subjects of known blood group and secretor status were obtained and their relative specificity for A, B, and H antigen was measured.

Patterns of enzyme specificity were found that were related to the ABO blood type of each subject. This was most evident for enzyme preparations of blood group A, B, and AB secretors: enzyme preparations from group A secretors rapidly degraded A antigen but degraded B antigen only slightly during the same time interval; enzyme preparations from group B secretors degraded B antigen rapidly and A antigen only slightly, and enzyme preparations from group AB secretors degraded both A and B antigens.

Bacterial adaptation of blood group A antigen-degrading enzyme activity was demonstrated in an in vitro anaerobic culture of fecal bacteria from a blood group B secretor.

These findings are compatible with enteric bacterial adaptation of degradative enzymes to the genetically determined blood group antigens in their host's gut mucous secretions.

Full text

PDF
664

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Carlson D. M. Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins. J Biol Chem. 1968 Feb 10;243(3):616–626. [PubMed] [Google Scholar]
  2. GLYNN L. E., HOLBOROW E. J. [Distribution of blood-group substances in human tissues]. Br Med Bull. 1959 May;15(2):150–153. doi: 10.1093/oxfordjournals.bmb.a069740. [DOI] [PubMed] [Google Scholar]
  3. HOWE C., MACLENNAN J. D., MANDL I., KABAT E. A. Enzymes of Clostridium tertium: effects on blood group and virus receptor substances. J Bacteriol. 1957 Sep;74(3):365–376. doi: 10.1128/jb.74.3.365-376.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hoskins L. C. Bacterial degradation of gastrointestinal mucins. II. Bacterial origin of fecal ABH(O) blood group antigen-destroying enzymes. Gastroenterology. 1968 Feb;54(2):218–224. [PubMed] [Google Scholar]
  5. Hoskins L. C., Zamcheck N. Bacterial degradation of gastrointestinal mucins. I. Comparison of mucus constituents in the stools of germ-free and conventional rats. Gastroenterology. 1968 Feb;54(2):210–217. [PubMed] [Google Scholar]
  6. LINDSTEDT G., LINDSTEDT S., GUSTAFSSON B. E. MUCUS IN INTESTINAL CONTENTS OF GERMFREE RATS. J Exp Med. 1965 Feb 1;121:201–213. doi: 10.1084/jem.121.2.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. Lloyd K. O., Kabat E. A., Licerio E. [Immunochemical studies on blood groups. 38. Structures and activities of oligosaccharides produced by alkaline degradation of blood-group Lewis-a substance. Proposed structure of the carbohydrate chains of human blood-group A, B, H, Le-a, and Le-b substances]. Biochemistry. 1968 Aug;7(8):2976–2990. doi: 10.1021/bi00848a039. [DOI] [PubMed] [Google Scholar]
  9. MARCUS D. M., KABAT E. A., SCHIFFMAN G. IMMUNOCHEMICAL STUDIES ON BLOOD GROUPS. XXXI. DESTRUCTION OF BLOOD GROUP A ACTIVITY BY AN ENZYME FROM CLOSTRIDIUM TERTIUM WHICH DEACETYLATES N-ACETYLGALACTOSAMINE IN INTACT BLOOD GROUP SUBSTANCES. Biochemistry. 1964 Mar;3:437–443. doi: 10.1021/bi00891a023. [DOI] [PubMed] [Google Scholar]
  10. NAYLOR I., BAER H. Studies of an enzyme produced by Bacillus fulminans that inactivates blood group O substance. J Bacteriol. 1959 Jun;77(6):771–775. doi: 10.1128/jb.77.6.771-775.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. SALM R., ADLINGTON S. R. Seminoma in identical twins. Br Med J. 1962 Oct 13;2(5310):964–965. doi: 10.1136/bmj.2.5310.964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. SPRINGER G. F., ROSE C. S., GYORGY P. Blood group mucoids: their distribution and growth-promoting properties for Lactobacillus bifidus var. Penn. J Lab Clin Med. 1954 Apr;43(4):532–542. [PubMed] [Google Scholar]
  13. STACK M. V., MORGAN W. T. J. The preparation and properties of enzymes from Clostridium welchii (type B) filtrates which destroy blood group substances. Br J Exp Pathol. 1949 Oct;30(5):470–483. [PMC free article] [PubMed] [Google Scholar]
  14. SZULMAN A. E. The histological distribution of blood group substances A and B in man. J Exp Med. 1960 Jun 1;111:785–800. doi: 10.1084/jem.111.6.785. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. WATKINS W. M. Enzymes of Trichomonas foetus; the action of cell-free extracts on blood-group substances and low-molecular-weight glycosides. Biochem J. 1959 Feb;71(2):261–274. doi: 10.1042/bj0710261. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Watkins W. M. Blood-group substances. Science. 1966 Apr 8;152(3719):172–181. doi: 10.1126/science.152.3719.172. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES