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Journal of Biochemistry Advance Access published online on April 13, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp062
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

The presence of OMP inclusion bodies in a Escherichia coli K-12 mutated strain is not related to lipopolysaccharide structure

M. Michela Corsaro1, Ermenegilda Parrilli1,2, Rosa Lanzetta1, Teresa Naldi1, Giuseppina Pieretti1, Buko Lindner3, Andrea Carpentieri1, Michelangelo Parrilli1 and M.Luisa Tutino1,2,*

1Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Napoli, Italy
2Facoltà di Scienze Biotecnologiche Università di Napoli Federico II
3Division of Immunochemistry, Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 10, D-23845 Borstel, Germany.

*Corresponding author: M.Luisa Tutino: Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cintia 4, 80126 Napoli, Italy; tel: 0039081674317 fax:0039081674313; e-mail: tutino{at}unina.it

Received May 30, 2009; Accepted April 2, 2009


  Abstract

The role of lipopolysaccharides in the biogenesis of outer membrane proteins have been investigated in several studies. Some of these analyses showed that lipopolysaccharide is required for correct and efficient folding of outer membrane proteins; other studies support the idea of independence of outer membrane proteins biogenesis from lipopolysaccharide structure. In this paper we investigated the involvement of lipopolysaccharide structure in the anomalous aggregation of outer membrane proteins in a E. coli mutant strain (S17-1({lambda}pir)). To achieve this aim, the lipopolysaccharide structure of the mutant strain was carefully determined and compared with the E. coli K-12 one. It turned out that lipopolysaccharide of these two strains differs in the inner core for the absence of a heptose residue (HepIII). We demonstrated that this difference is due to a mutation in waaQ, a gene encoding the transferase for the branch heptose HepIII residue. The mutation was complemented to find out if the restoration of lipopolysaccharide structure influenced the observed outer membrane proteins aggregation. Data reported in this work demonstrated that, in E. coli S17-1({lambda}pir) there is no an influence of lipopolysaccharides structure on the outer membrane proteins inclusion bodies formation.

Key Words: E. coli S17-1 ({lambda}pir), inclusion bodies, LPS structures, Fourier-transform mass spectrometry, NMR spectroscopy


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