Biorecognition of Escherichia coli K88 adhesin for glycated porcine albumin

Andre i. Sarabia-Sainz, Gabriela Ramos-Clamont, Ma María del Carmen Candia-Plata, Luz Vázquez-Moreno

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

14 Citas (Scopus)

Resumen

Escherichia coli (E. coli) that expresses galactose-reactive lectins, like K88 adhesin, causes high mortality among piglets. Carbohydrates that compete for adhesion could serve as an alternative for disease prevention. Porcine serum albumin (PSA) was modified by non-enzymatic glycation with lactose to produce PSA-Lac or PSA-Glc β (1-4) Gal, as confirmed by reduction of available free amino groups, increased molecular mass and by Ricinus communis lectin recognition. E. coli K88 binds to PSA-Lac treatments containing three and four lactoses, respectively. In addition, PSA-Lac partially inhibited K88 strain adherence to mucins. These results suggest that neoglycoconjugates obtained by non-enzymatic glycation of proteins may serve in the prophylaxis of piglets' diarrhea. © 2009 Elsevier B.V. All rights reserved.
Idioma originalInglés estadounidense
Páginas (desde-hasta)175-181
Número de páginas7
PublicaciónInternational Journal of Biological Macromolecules
DOI
EstadoPublicada - 1 mar 2009

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