Журнал гликомики и липидомики
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Lectin Array Analysis of Purified Lipooligosaccharide: A Method for the Determination of Molecular Mimicry

Evgeny A Semchenko, Marc Moutin, Victoria Korolik, Joe Tiralongo and Christopher J Day

Surface glycosylation of bacteria is involved in many critical host-microbe interactions. Lectin arrays consisting of diverse carbohydrate binding proteins have proven to be an important tool for evaluating a wide variety of glycosylation, including that present on whole bacteria. However, assessing glycosylation on whole bacteria using lectin arrays may not reflect bacterial glycosylation, but interactions between bacteria and the glycosylation present on lectins. The lipooligosaccharide of Campylobacter jejuni NCTC 11168 and 81-176 are known to mimic the human monosialylated gangliosides. This molecular mimicry by C. jejuni can result in the post infection sequelae Guillain–Barré syndrome. Using C. jejuni as a model system and a discreet lectin and antibody array, a method, applicable to many organisms has been developed and validated by to screening of the purified lipooligosaccharide of C. jejuni for molecular mimicry to monosialylated gangliodises. In case of C. jejuni, knowing whether clinically important bacterial strains are capable of inducing severe autoimmune responses may aid in prevention and/or early diagnosis of debilitating post infection conditions.