Recognition of flavin mononucleotide, Haemophilus influenzae type b and its capsular polysaccharide vaccines by antibodies specific to D-ribitol-5-phosphate
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- 作者：G. Ravi (1)
Yeldur P. Venkatesh (1) - 关键词：Capsular polysaccharide ; Conjugate vaccine ; Haemophilus influenzae type b ; Immunogenicity ; Polyribosyl ribitol phosphate ; Ribitol ; 5 ; phosphate–specific antibodies
- 刊名：Glycoconjugate Journal
- 出版年：2014
- 出版时间：November 2014
- 年：2014
- 卷：31
- 期：8
- 页码：573-585
- 全文大小：3,173 KB
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Yeldur P. Venkatesh (1)
1. Department of Biochemistry and Nutrition, CSIR–Central Food Technological Research Institute (CFTRI), ‘Chaluvamba Vilas- KRS Road, Mysore, 570020, Karnataka State, India - ISSN：1573-4986
文摘
D-Ribitol-5-phosphate (Rbt-5-P) is an important metabolite in the pentose phosphate pathway and an integral part of bacterial cell wall polysaccharides, specifically as polyribosyl ribitol phosphate (PRP) in Haemophilus influenzae type b (Hib). The major objective of this study was to investigate whether an antibody specific to Rbt-5-P can recognize the PRP of Hib. D-Ribose-5-phosphate was reacted with proteins in the presence of sodium cyanoborohydride to obtain Rbt-5-P epitopes; 120?h reaction resulted in conjugation of ~30 and ~17 moles of Rbt-5-P/mole of BSA and OVA, respectively, based on decrease in amino groups, MALDI–TOF analyses, an increase in apparent molecular weight (SDS–PAGE) and glycoprotein staining. Immunization of rabbits with Rbt-5-P–BSA conjugate generated antibodies to Rbt-5-P as demonstrated by dot immunoblot and non-competitive ELISA. Homogeneous Rbt-5-P-specific antibody was purified from Rbt-5-P–BSA antiserum subjected to caprylic acid precipitation followed by hapten–affinity chromatography; its affinity constant is 7.1?×-08?M?. Rbt-5-P antibody showed 100?% specificity to Rbt-5-P, ~230?%, 10?% and 3.4?% cross-reactivity to FMN, riboflavin and FAD, respectively; the antibody showed ~4?% cross-reactivity to D-ribitol and Hib conjugate vaccines containing PRP which was inhibited specifically by Rbt-5-P, and also detected Hib cell-surface capsular polysaccharides by immunofluorescence. In conclusion, Rbt-5-P–protein conjugate used as an immunogen elicited antibodies binding to an epitope also present in PRP and Hib bacteria. Rbt-5-P–specific antibody has potential applications in the detection and quantification of free/bound Rbt-5-P and FMN as well as immunological recognition of Hib bacteria and its capsular polysaccharide.