4.7 Article

Analysis of outer membrane protein complexes and heat-modifiable proteins in Neisseria strains using two-dimensional diagonal electrophoresis

Journal

JOURNAL OF PROTEOME RESEARCH
Volume 4, Issue 1, Pages 91-95

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/pr049846i

Keywords

Neisseria meningitidis; Neisseria lactamica; porins; membrane complexes; mobility shift; diagonal electrophoresis

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Two-dimensional diagonal SDS-PAGE was used to resolve membrane complexes and identify proteins with temperature-dependent mobility in Neisseria meningitidis and N. lactamica. The main membrane complexes were composed of porins and were formed by heteromers of PorA, PorB and RmpM in N. meningitidis, and by PorB and RmpM in N. lactamica. Also, other proteins, including Opa, with temperature-dependent mobility were clearly demonstrated. The method allows improved detection of the components of membrane complexes and proteins with temperature-dependent mobility which is difficult to resolve with other analytical approaches.

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