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Title: Colony morphology variation of Burkholderia pseudomallei is associated with antigenic variation and O-polysaccharide modification
Authors: Chanthiwa Wikraiphat
Natnaree Saiprom
Sarunporn Tandhavanant
Christian Heiss
Parastoo Azadi
Gumphol Wongsuvan
Apichai Tuanyok
Matthew T.G. Holden
Mary N. Burtnick
Paul J. Brett
Sharon J. Peacock
Narisara Chantratita
Mahidol University
The University of Georgia
University of Hawaii at Manoa
Wellcome Trust Sanger Institute
University of South Alabama
University of Cambridge
Keywords: Immunology and Microbiology
Issue Date: 1-Jan-2015
Citation: Infection and Immunity. Vol.83, No.5 (2015), 2127-2138
Abstract: © 2015, American Society for Microbiology. Burkholderia pseudomallei is a CDC tier 1 select agent that causes melioidosis, a severe disease in humans and animals. Persistent infections are common, and there is currently no vaccine available. Lipopolysaccharide (LPS) is a potential vaccine candidate. B. pseudomallei expresses three serologically distinct LPS types. The predominant O-polysaccharide (OPS) is an unbranched heteropolymer with repeating D-glucose and 6-deoxy-L-talose residues in which the 6-deoxy-L-talose residues are variably replaced with O-acetyl and O-methyl modifications. We observed that primary clinical B. pseudomallei isolates with mucoid and nonmucoid colony morphologies from the same sample expressed different antigenic types distinguishable using an LPS-specific monoclonal antibody (MAb). MAb-reactive (nonmucoid) and nonreactive (mucoid) strains from the same patient exhibited identical LPS banding patterns by silver staining and indistinguishable genotypes. We hypothesized that LPS antigenic variation reflected modification of the OPS moieties. Mutagenesis of three genes involved in LPS synthesis was performed in B. pseudomallei K96243. Loss of MAb reactivity was observed in both wbiA (encoding a 2-O-acetyltransferase) and wbiD (putative methyl transferase) mutants. The structural characteristics of the OPS moieties from isogenic nonmucoid strain 4095a and mucoid strain 4095c were further investigated. Utilizing nuclear magnetic resonance (NMR) spectroscopy, we found that B. pseudomallei 4095a and 4095c OPS antigens exhibited substitution patterns that differed from the prototypic OPS structure. Specifically, 4095a lacked 4-O-acetylation, while 4095c lacked both 4-O-acetylation and 2-O-methylation. Our studies indicate that B. pseudomallei OPS undergoes antigenic variation and suggest that the 9D5 MAb recognizes a conformational epitope that is influenced by both O-acetyl and O-methyl substitution patterns.
ISSN: 10985522
Appears in Collections:Scopus 2011-2015

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