Relative intensities of recognition factors at two combining sites of Ralstonia solanacearum lectin (RSL) for accommodating lFucα1→, dManα1→ and Galβ1→3/4GlcNAc glycotopes

Abstract

Owing to the weak reactivities of monomeric dManα1 and Galβ1→3/4GlcNAcβ (I β/II β) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes lFucα1→, dManα1→ and I β/II β within two combining sites were established by both enzyme‐linked lectinosorbent and inhibition assays. It was found that high density of lFucα1→ complex enhanced the recognition intensities at lFucα1→ site, polyvalent dManα1→ was essential for binding at the dManα1→ site and polyvalent I β/II β was required at lFucα1→ site. The peculiar recognition systems of RSL are very different from other well known microbial lectins.

Synthesis and characterization of Schiff base analogues of fluoroaniline and their antibiocidal activity against MRSA

“…S. aureus communicates unmistakable surface proteins that are basic for official to have cells to go about as destructiveness factors 16,17 . These surface proteins normally elevate connection to laminin and fibronectin 18 . Most strains likewise express an amassing factor, coagulase protein response, which elevates connection to blood clusters.…”