Bacterial recognition of thermal glycation products derived from porcine serum albumin with lactose

• Autorzy: Sarabia-Sainz A. , Ramos-Clamont G. , Winzerling J. , Vazquez-Moreno L.
• Języki publikacji: EN

Abstrakty

EN

 Recently, glyco-therapy is proposed to prevent the interaction of bacterial lectins with host ligands (glycoconjugates). This interaction represents the first step in infection. Neoglycans referred to as PSA-Lac (PSA-Glu (β1-4) Gal) were obtained by conjugation of porcine serum albumin (PSA) with lactose at 80 °C, 100 °C and 120 ºC. Characterization studies of the products showed that PSA could contain 1, 38 or 41 added lactoses, depending on the reaction temperature. These neoglycans were approximately 10 times more glycated than PSA-Lac obtained in previous work. Lactose conjugation occurred only at lysines and PSA-Lac contained terminal galactoses as confirmed by Ricinus communis lectin recognition. Furthermore, Escherichia coli K88+, K88ab, K88ac and K88ad adhesins showed affinity toward all PSA-Lac neoglycans, and the most effective was the PSA-Lac obtained after 100 ºC treatment. In vitro, this neoglycan partially inhibited the adhesion of E. coli K88+ to piglet mucin (its natural ligand). These results provide support for the hypothesis that glycated proteins can be used as an alternative for bioactive compounds for disease prevention.

Słowa kluczowe

EN

Escherichia coli; adhesion; albumin; bacterial recognition; glycation; high performance liquid chromatography; lactose; neoglycan; porcine serum albumin; serum albumin; thermal glycation product; disease prevention

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2011
• Tom: 58
• Numer: 1
• Opis fizyczny: p.95-100,fig.,ref.

Twórcy

autor

Sarabia-Sainz A.

• Laboratorio de Bioquímica de Proteínas, Coordinación de Ciencia de los Alimentos, Centro de Investigación en Alimentación y Desarrollo A.C. (CIAD A.C.), Hermosillo, Sonora, Mexico

autor

Ramos-Clamont G.

autor

Winzerling J.

autor

Vazquez-Moreno L.

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