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

Hoskins, Lansing C.

doi:10.1172/jci106024

Cited by 26 publications

(18 citation statements)

References 18 publications

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“…The result should be an increased population density of that strain. This was the case for bacteria producing blood group B-degrading activity in B secretors (18) and is a presumed mechanism for the greater levels of B-degrading activity observed in fecal extracts (35) and whole fecal cultures (17) of blood group B secretors.…”

Section: Discussionmentioning

confidence: 90%

Mucin degradation in human colon ecosystems. Isolation and properties of fecal strains that degrade ABH blood group antigens and oligosaccharides from mucin glycoproteins.

Hoskins¹,

Agustines²,

McKee³

et al. 1985

J. Clin. Invest.

299

193

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We previously reported that the oligosaccharide chains of hog gastric mucin were degraded by unidentified subpopulations numbering 1% of normal human fecal bacteria. Here we report on the enzyme-producing properties of five strains of mucin oligosaccharide chain-degrading bacteria isolated from feces of four healthy subjects. Four were isolated from the greatest fecal dilutions yielding mucin side chain-degrading activity in culture, and thus were the numerically dominant side chain-degrading bacteria in their respective hosts. Three were Ruminococcus strains and two were Bifidobacterium strains. Two Ruminococcus torques strains, IX-70 and VIII-239, produced blood group A-and H-degrading a-glycosidase activities, sialidase, and the requisite jl-glycosidases; these strains released >90% of the anthrone-reacting hexoses from hog gastric mucin during growth in culture. The Bifidobacterium strains lacked A-degrading activity but were otherwise similar, these released 60-80% of the anthrone-reacting hexoses but not the A antigenic structures from hog gastric mucin. Only Ruminococcus AB strain VI-268 produced blood group B-degrading a-galactosidase activity, but this strain lacked ,5-N-acetyl exosaminidases to complete degradation of B antigenic chains. When this strain was co-cultured with a strain that produced jl-N-acetylhexosaminidases, release of hexoses from blood group B salivary glycoprotein increased from 50 to >90%, and bacterial growth was enhanced. The glycosidases required for side chain degradation were produced by these strains in the absence of mucin substrate, and a substantial fraction of each activity in stationary phase cultures was extracellular. In contrast, none of 16 other fecal Bacteroides, Escherichia coli, Streptococcus faecalis, and Bifidobacterium strains produced ABH blood group-degrading enzymes; other glycosidases produced by these strains were predominantly cell bound except for extracellular j-N-acetylhexosaminidases produced by the five S. faecalis strains.We conclude that certain Bifidobacterium and Ruminococcus strains are numerically dominant populations degrading mucin oligosaccharides in the human colon due to their constitutive production of the requisite extracellular glycosidases including blood group antigen-specific a-glycosidases. These properties characterize them as a functionally distinct subpopulation of normal human enteric microflora comprised of An abstract of portions of this work was published in Gastroenterology 1983; 84:1191.

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Section: Discussionmentioning

confidence: 90%

Mucin degradation in human colon ecosystems. Isolation and properties of fecal strains that degrade ABH blood group antigens and oligosaccharides from mucin glycoproteins.

Hoskins¹,

Agustines²,

McKee³

et al. 1985

J. Clin. Invest.

299

193

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“…Stools were obtained from healthy subjects. Each subject's blood type and ABH salivary secretor status was determined as described previously (20).…”

Section: Methodsmentioning

confidence: 99%

“…We earlier reported (20) that the host's blood type and secretor status influenced the specificity of A-, B-, and H-degrading activities in feces. The present studies indicate that these genetic traits also influence the specificity of BGD enzymes produced in anaerobic fecal cultures.…”

Section: Methodsmentioning

confidence: 99%

“…Fecal BGD enzymes were shown to originate from enteric bacteria and not from the host (18); they presumably had a role in the extensive degradation of the carbohydrate moieties of mucin glycoproteins by enteric bacteria (19). It was shown that BGD enzyme activity in fecal extracts from individual ABH secretors was generally greatest for the host's blood group phenotype antigen (20). This suggests that the enteric microflora adapts degradative enzymes to the blood group antigenic structures in the gut mucins secreted by the host.…”

Section: Introductionmentioning

confidence: 99%

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Degradation of blood group antigens in human colon ecosystems. I. In vitro production of ABH blood group-degrading enzymes by enteric bacteria.

Hoskins¹,

Boulding²

1976

J. Clin. Invest.

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A B S T R A C T Human feces contain enzymes producedby enteric bacteria that degrade the A, B, and H blood group antigens of gut mucin glycoproteins. We have studied their production in fecal cultures to determine if such cultures can be a source for enzyme purification and to explore how blood group antigen-degrading enzymes are adapted in individual human colon ecosystems. They were present in fecal cultures from each of 27 healthy subjects, including ABH nonsecretors. Heatsensitive obligate anaerobes are their major source. From 39 to 85% of the total enzyme activity produced by growing cultures was extracellular. Commercial hog gastric mucin and salivary glycoproteins, including Le' saliva which lacks A, B, and H antigens, enhance production of A-, B-, and H-degrading activity in anaerobic fecal cultures irrespective of the glycoprotein's blood group specificity. There is evidence that the host's ABO blood type and secretor status affects the specificity of blood group-degrading enzymes produced by his fecal bacteria in vitro. Thus, fecal inocula from B secretors incubated with hog gastric mucin (A and H specificity) or with Lea saliva produced greater levels of B-degrading than A-or H-degrading activity, and inocula from A secretors in similar media produced greater levels of A-degrading than B-or H-degrading activity. Blood group-degrading enzymes produced in fecal cultures are glycosidases and not proteases. The B-degrading enzyme cleaves the B antigenic determinant a-D-galactose A portion of this work was presented in abstract form in 1972. Clin. Res. 20: 728.

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“…Blood group-degrading enzymes produced by fecal bacteria from conventional rats and normal individuals have been shown to modify the blood group antigenicity of hog gastric mucin by removing terminal sugars of the oligosaccharide chains (1,2). Recently, we have identified a similar blood group B-degrading enzyme in cecal contents of normal rats.…”

Section: Introductionmentioning

confidence: 99%

Glycoprotein Degradation in the Blind Loop Syndrome

Prizont¹

1981

J. Clin. Invest.

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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

Abstract: A B S T R A C T This report

Cited by 26 publications

References 18 publications

Mucin degradation in human colon ecosystems. Isolation and properties of fecal strains that degrade ABH blood group antigens and oligosaccharides from mucin glycoproteins.

Mucin degradation in human colon ecosystems. Isolation and properties of fecal strains that degrade ABH blood group antigens and oligosaccharides from mucin glycoproteins.

Degradation of blood group antigens in human colon ecosystems. I. In vitro production of ABH blood group-degrading enzymes by enteric bacteria.

Glycoprotein Degradation in the Blind Loop Syndrome

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