Recognition of riboflavin and the capsular polysaccharide of Haemophilus influenzae type b by antibodies generated to the haptenic epitope D-ribitol
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- 作者：G. Ravi (1)
Yeldur P. Venkatesh (1) - 关键词：Haemophilus influenzae type b ; Immunogenicity ; Polyribosyl ribitol phosphate ; Reductive amination ; Ribitol–specific antibodies ; Riboflavin
- 刊名：Glycoconjugate Journal
- 出版年：2014
- 出版时间：April 2014
- 年：2014
- 卷：31
- 期：3
- 页码：247-258
- 全文大小：2,954 KB
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Yeldur P. Venkatesh (1)
1. Department of Biochemistry and Nutrition, CSIR–Central Food Technological Research Institute, ‘Chaluvamba Vilas- KRS Road, Mysore, 570020, Karnataka State, India - ISSN：1573-4986
文摘
D-Ribitol, a five–carbon sugar alcohol, is an important metabolite in the pentose phosphate pathway; it is an integral part of riboflavin (vitamin B2) and cell wall polysaccharides in most Gram-positive and a few Gram-negative bacteria. Antibodies specific to D-ribitol were generated in New Zealand white rabbits by using reductively aminated D-ribose-BSA conjugate as the immunogen. MALDI-TOF and amino group analyses of ribitol-BSA conjugate following 120?h reaction showed ~27-0?mol of ribitol conjugated per mole BSA. The presence of sugar alcohol in the conjugates was also confirmed by an increase in molecular mass and a positive periodic acid–Schiff staining in SDS-PAGE. Caprylic acid precipitation of rabbit serum followed by hapten affinity chromatography on ribitol–KLH–Sepharose CL-6B resulted in pure ribitol–specific antibodies (~45-0?μg/mL). The affinity constant of ribitol antibodies was found to be 2.9?×-07?M? by non-competitive ELISA. Ribitol antibodies showed 100?% specificity towards ribitol, ~800?% cross–reactivity towards riboflavin, 10-5?% cross–reactivity with sorbitol, xylitol and mannitol, and 5-?% cross–reactivity with L-arabinitol and meso-erythritol. The specificity of antibody to ribitol was further confirmed by its low cross-reactivity (0.4?%) with lumichrome. Antibodies to D-ribitol recognized the purified capsular polysaccharide of Haemophilus influenzae type b, which could be specifically inhibited by ribitol. In conclusion, antibodies specific to D-ribitol have been generated and characterized, which have potential applications in the detection of free riboflavin and ribitol in biological samples, as well as identification of cell-surface macromolecules containing ribitol.