The outer membrane protein A (OmpA) and the acyl carrier protein (ACP) are virulence determinants of Burkholderia cenocepacia J2315

December 2007

Aiming at the identification of new virulence factors that might be exploited to develop new methods for early detection of respiratory infections caused by Burkholderia cepacia complex (Bcc) in cystic fibrosis (CF) patients or/and to be used as potential therapeutic targets to control Bcc infections, a collection of mutants derived from the virulent CF isolate B. cenocepacia J2315 was constructed by random plasposon mutagenesis, using previously established techniques (1,2). The screening of this collection of mutants allowed the identification of two mutants (FA1 and FA2) with impaired virulence to the nematode Caenorhabditis elegans. This nematode was previously shown to be a useful host model to study Bcc pathogenesis (3). Cloning and sequence analysis of the interrupted genes in both B. cenocepacia J2315 mutants revealed that mutant FA1 has a mutation in a gene encoding a putative outer membrane protein A (OmpA) presumably playing a structural role in the integrity of the bacterial cell surface. Mutant FA2 has a mutation in a gene encoding a putative acyl carrier protein (ACP). ACPs have a central role in the type II biosynthetic pathway of fatty acids and in other diverse metabolic pathways of bacteria (e.g. phospholipids, lipid A, acylated homoserine lactones). Results on the functional analysis of these two proteins will be presented.

Authors in the community:

• 

  S

  Sílvia Andreia Bento da Silva Sousa Barbosa

  ist90151

• 

  J

  Jorge Humberto Gomes Leitão

  ist14034

  Affiliations and sources

  IST > iBB

  Instituto de Bioengenharia e Biociências

  IST > DBE

  Departamento de Bioengenharia

This information is not available. Please contact the author for more information.

Lisboa, Portugal

biological-sciences - Biological sciences

eng - English