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Identification of a novel two-partner secretion system from<Emphasis Type="Italic"> Burkholderia pseudomallei</Emphasis>
Authors:N?F?Brown  C-A?Logue  J?A?Boddey  R?Scott  R?G?Hirst  Email author" target="_blank">I?R?BeachamEmail author
Institution:(1) School of Health Science, Griffith University-Gold Coast Campus, PMB 50 Gold Coast Mail Centre, QLD 4217 Gold Coast, Queensland, Australia;(2) Department of Microbiology and Immunology, James Cook University, QLD 4811 Townsville, Queensland, Australia;(3) Present address: Biotechnology Laboratory, University of British Columbia, 237-6174 University Boulevard, Vancouver, British Columbia, V6T 1Z3, Canada
Abstract:Two adjacent genes, bpaA and bpaB, whose products display significant similarity to a number of two-partner secretion (TPS) systems have been identified in Burkholderia pseudomallei strain 08, but are absent from the closely related avirulent species B. thailandensis. They possess a number of sequence features characteristic of TPS systems, including the presence of an NPNGI motif in a region of BpaA which strongly resembles a TPS secretion domain. BpaA is a very large protein (~530 kDa) and contains three repeats, each 600–800-amino acids long. Putative membrane-spanning regions in BpaB were identified through alignment with TpsB family members, and this also revealed an N-terminal extension not found in other TpsB proteins. The bpaA gene was found to be absent from the majority of B. pseudomallei strains. It appears that bpaAB are located within a putative genomic island that is inserted in close proximity to a methionine tRNACAT-encoding gene. Expression of BpaA was undetectable in cells grown in laboratory media. However, owing to the similarity of BpaA to known adhesin molecules, a potential role of BpaA in virulence was investigated in cell culture and in an animal model, but no evidence for such a role was found in these test systems.Communicated by W. Goebel
Keywords: Burkholderia pseudomallei  Secretion  Deletion mutagenesis  DNA sequence
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