The effect of sialidase on transferrins and other serum proteins

Blumberg, Baruch S.; Warren, Irene

doi:10.1016/0006-3002(61)91064-2

Cited by 66 publications

(13 citation statements)

References 17 publications

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“…Many studies have demonstrated that microbial neuraminidases have the capacity to modify the ability of the host to respond to infection (for review see [2]). The ¢nding of neuraminidase activity in crude diphtherial toxin preparations was reported by Blumberg and Warren [4]. The enzyme was characterized by Warren and Spearing [5] and Jamieson [6] suggesting a molecular mass of about 50 000 and 100 000, respectively.…”

Section: Introductionmentioning

confidence: 99%

trans-Sialidase activity for sialic acid incorporation on Corynebacterium diphtheriae

Mattos‐Guaraldi

1998

FEMS Microbiology Letters

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A rapid and sensitive assay for neuraminidase using peanut lectin hemagglutination was used to study the prevalence of neuraminidase activity among sucrose-fermenting and non-sucrose-fermenting toxigenic Corynebacterium diphtheriae strains. Neuraminidase activity was found in 15 (100%) isolates regardless of biotype, hemagglutinating activity and site of isolation of bacteria. Besides expressing the neuraminidase activity that hydrolyzes sialic acid from glycoconjugates, C. diphtheriae was also capable of transferring sialic acid residues from a sialyl-lactose donor. A single molecule probably expresses both neuraminidase and trans-sialidase activity. The trans-sialidase activity was documented by observations of the interactions of bacterial cells with wheat germ agglutinin and peanut lectins. C. diphtheriae expressed a trans-sialidase activity located on the cell surface that produced asialoglycoconjugates from a sialyl donor substrate and at the same time generated bacterial sialyl derivatives of L-Gal acceptors. z

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Section: Introductionmentioning

confidence: 99%

trans-Sialidase activity for sialic acid incorporation on Corynebacterium diphtheriae

Mattos‐Guaraldi

1998

FEMS Microbiology Letters

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“…After exposure to neuraminidase at pH 5.5, as recommended by Blumberg and W a r ren [3], the C'-fixing activity of heated or unheated IgG was completely abolished at the protein concentration of 4 mg/0.2 ml. It was found, however, that this loss of activity was entirely attributable to the acid pH of the incubation medium, and not to the effect of the neuraminidase.…”

Section: Resultsmentioning

confidence: 99%

Effect of Neuraminidase and Acidification on Complement-Fixing Properties of Human IgA and IgG

Vaerman¹,

Heremans²

1968

Int Arch Allergy Immunol

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“…Several workers report th at differences in sialic acid content do not account for complex transferrin phenotypes of mammals (Gordon and Louis [1963]; Parker and Bearn [1962]; Blumberg and Warren [1961]). These reports are not supported by our work.…”

Section: Discussionmentioning

confidence: 99%