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Journal of Biochemistry Advance Access originally published online on April 13, 2009
Journal of Biochemistry 2009 146(2):231-240; 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, Complesso Universitario di Monte Sant'Angelo - Via Cinthia 80126 Napoli; and 3Division of Immunochemistry, Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 10, D-23845 Borstel, Germany

*To whom correspondence should be addressed. Tel: +39-081-674317, Fax: +39-081-674313, E-mail: tutino{at}unina.it

Received March 30, 2009; Accepted April 2, 2009


  Abstract

The role of lipopolysaccharides (LPSs) in the biogenesis of outer membrane proteins have been investigated in several studies. Some of these analyses showed that LPS is required for correct and efficient folding of outer membrane proteins; other studies support the idea of independence of outer membrane proteins biogenesis from LPS structure. In this article, we investigated the involvement of LPS structure in the anomalous aggregation of outer membrane proteins in a E. coli mutant strain (S17-1({lambda}pir)). To achieve this aim, the LPS structure of the mutant strain was carefully determined and compared with the E. coli K-12 one. It turned out that LPS 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 LPS 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 influence of LPS structure on the outer membrane proteins inclusion bodies formation.

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

Abbreviations: DQF-COSY, double quantum filtered-correlation spectroscopy; GC-MS, gas chromatography-mass spectrometry; HMBC, heteronuclear multiple bond correlation; HSQC-DEPT, heteronuclear single quantum coherence-distortionless enhancement by polarization transfer; Kdo, 3-deoxy-D-manno-oct-2-ulosonic acid; ROESY, rotating-frame nuclear Overhauser effect spectroscopy; TOCSY, total correlation spectroscopy


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