Deciphering minimal antigenic epitopes associated with Burkholderia pseudomallei and Burkholderia mallei lipopolysaccharide O-antigens

Marielle Tamigney Kenfack, Marcelina Mazur, Teerapat Nualnoi, Teresa L. Shaffer, Abba Ngassimou, Yves Blériot, Jérôme Marrot, Roberta Marchetti, Kitisak Sintiprungrat, Narisara Chantratita, Alba Silipo, Antonio Molinaro, David P. AuCoin, Mary N. Burtnick, Paul J. Brett () and Charles Gauthier ()
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Marielle Tamigney Kenfack: Université de Poitiers
Marcelina Mazur: Université de Poitiers
Teerapat Nualnoi: University of Nevada School of Medicine
Teresa L. Shaffer: University of South Alabama
Abba Ngassimou: Université de Poitiers
Yves Blériot: Université de Poitiers
Jérôme Marrot: Université de Versailles Saint-Quentin-en-Yvelines, Université Paris-Saclay
Roberta Marchetti: Università di Napoli Federico II, Complesso Universitario Monte S. Angelo
Kitisak Sintiprungrat: Mahidol University
Narisara Chantratita: Mahidol University
Alba Silipo: Università di Napoli Federico II, Complesso Universitario Monte S. Angelo
Antonio Molinaro: Università di Napoli Federico II, Complesso Universitario Monte S. Angelo
David P. AuCoin: University of Nevada School of Medicine
Mary N. Burtnick: University of South Alabama
Paul J. Brett: University of South Alabama
Charles Gauthier: Université de Poitiers

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: Abstract Burkholderia pseudomallei (Bp) and Burkholderia mallei (Bm), the etiologic agents of melioidosis and glanders, respectively, cause severe disease in both humans and animals. Studies have highlighted the importance of Bp and Bm lipopolysaccharides (LPS) as vaccine candidates. Here we describe the synthesis of seven oligosaccharides as the minimal structures featuring all of the reported acetylation/methylation patterns associated with Bp and Bm LPS O-antigens (OAgs). Our approach is based on the conversion of an l-rhamnose into a 6-deoxy-l-talose residue at a late stage of the synthetic sequence. Using biochemical and biophysical methods, we demonstrate the binding of several Bp and Bm LPS-specific monoclonal antibodies with terminal OAg residues. Mice immunized with terminal disaccharide–CRM197 constructs produced high-titer antibody responses that crossreacted with Bm-like OAgs. Collectively, these studies serve as foundation for the development of novel therapeutics, diagnostics, and vaccine candidates to combat diseases caused by Bp and Bm.

Date: 2017
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DOI: 10.1038/s41467-017-00173-8

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