PapG adhesin from E. coli J96 recognizes the same saccharide epitope when present on whole bacteria and as isolated protein

• Purified PapG adhesin from the genetically well-defined uropathogenic Escherichia coli strain J96, as well as whole bacteria, were bound to microtiter plates that carried covalently bound globotetraose and galabiose. The binding was inhibited by soluble saccharide derivatives corresponding to the globoseries of glycolipids, including all di-, tri-, tetra-, and pentasaccharide fragments of the Forssman antigen and all monodeoxy analogues of galabiose. Analysis of the inhibition pattern showed no significant difference between purified adhesin and whole bacteria. The glucose unit at the reducing end of the natural saccharides was detrimental to PapG binding since deletion of the glucose unit increased the inhibitory power 10-20 fold. The five hydroxyl groups HO-6, -2', -3', -4', -6' of the galabiose unit were shown to be important for PapG binding, presumably via intermolecular hydrogen bonds.

Ämnesord

NATURVETENSKAP  -- Kemi -- Organisk kemi (hsv//swe)

NATURAL SCIENCES  -- Chemical Sciences -- Organic Chemistry (hsv//eng)

Nyckelord

E. coli J96

Forssman-related saccharides

Galabiose binding epitope

Microtiter plate ELISA

PapG adhesin

Publikations- och innehållstyp

art (ämneskategori)

ref (ämneskategori)