Analysis of outer membrane protein complexes and heat-modifiable proteins in Neisseria strains using two-dimensional diagonal electrophoresis.
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.
Sánchez
Sandra
S
Departamento de Microbiología, Facultad de Farmacia, Universidad de Santiago, 15782 Santiago de Compostela, Spain.
Arenas
Jesús
J
Abel
Ana
A
Criado
María-Teresa
MT
Ferreirós
Carlos M
CM
D001425:Bacterial Outer Membrane Proteins / Q000032:analysis*; D001426:Bacterial Proteins / Q000032:analysis; D015180:Electrophoresis, Gel, Two-Dimensional; D006358:Hot Temperature; D046912:Multiprotein Complexes / Q000032:analysis; D009343:Neisseria / Q000737:chemistry*; D018272:Porins / Q000032:analysis; D040901:Proteomics
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D046912:Multiprotein Complexes; D018272:Porins; C051591:Rmp protein, Neisseria; C090348:Opa protein, Neisseria