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

Hoskins, Lansing C.; Boulding, Erwin T.

doi:10.1172/jci108270

Cited by 86 publications

(46 citation statements)

References 29 publications

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“…Extensive loss (>70%) of HGM hexoses occurred in 95% of cultures containing either three or four of the glycosidases, and was greatest in those containing all four glycosidases (median loss of mucin hexoses = 95%, range = 79-99%). (17,18). Like other members of these genera, growth of each was enhanced by carbohydrates including glucose which were fermented with production of acid.…”

Section: Resultsmentioning

confidence: 99%

“…Enzyme assays were performed as previously described (16,17) on the culture supernate and on the bacterial sonicate fraction of each culture representing, respectively, extracellular and cell-bound enzyme activity. Blood group A-, B-, and H-antigen degrading activities were measured by the rate of decrease of the hemagglutination inhibition titer of each antigen substrate during incubation with culture fractions.…”

Section: Methodsmentioning

confidence: 99%

“…Bacterial protein concentration was the sum of the protein concentrations of the cell sonicate and cell residue. ABO blood group and secretor status of subjects were determined using standard hemagglutination techniques as previously described (17 …”

Section: Methodsmentioning

confidence: 99%

“…Chain degradation appeared to be dependent upon production of extracellular but not cell-bound sialidase, fl-galactosidase, and ,B-N-acetylglucosaminidase (16). Results of earlier studies indicated that extracellular a-glycosidases capable of degrading the ABH blood group antigens were also produced by unidentified subpopulations of normal human fecal bacteria (17,18).…”

Section: Introductionmentioning

confidence: 99%

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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.

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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: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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.

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300

193

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“…Mucin-degrading bacteria can adapt to the host mucins by producing specific enzymes, which are able to degrade the histo-blood group antigens (oligosaccharides). [107][108][109] Due to their high complexity and diversity, mucins can only be completely degraded by a panel of diverse enzymes, including proteases, glycosidases, sialidases and sulfatases, together designated as 'mucinases'. 109,110 Mucin degradation in vivo starts probably with cleavage of the non-glycosylated regions of the polypeptide backbone performed by proteolytic enzymes (Fig.…”

mentioning

confidence: 99%