Carbohydrate-reactive, pore-forming outer membrane proteins of Aeromonas hydrophila
| Autor: | Diana Quinn, M. Tester, A. H. Bretag, H. M. Atkinson, T. J. Trust, C. Y. F. Wong, Robert L. Flower |
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| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
Immunology Carbohydrates Porins Maltoporin Biology Microbiology Ion Channels Affinity chromatography Outer membrane efflux proteins Virulence biochemical phenomena metabolism and nutrition General bacterial porin family Aeromonas hydrophila Infectious Diseases Membrane Carbohydrate Sequence Biochemistry Membrane protein Porin Receptors Virus bacteria Parasitology Water Microbiology Bacterial outer membrane Bacterial Outer Membrane Proteins Research Article |
| Zdroj: | Infection and Immunity. 62:4054-4058 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.62.9.4054-4058.1994 |
| Popis: | Two outer membrane proteins of Aeromonas hydrophila A6, isolated in a one-step affinity chromatography process based on carbohydrate reactivity, were found to be pore-forming molecules in artificial planar bilayer membranes. These carbohydrate-reactive outer membrane proteins (CROMPs; M(r)s, 40,000 and 43,000) were subjected to amino acid analysis. The amino acid profiles for these two outer membrane proteins were almost identical. A partial protein sequence of a 14-amino-acid fragment of the 40,000-Da protein revealed homology with outer membrane porins of Escherichia coli and A. hydrophila. CROMPs were compared with carbohydrate-reactive porins also extracted from outer membranes of A. hydrophila A6. These porins were isolated by using standard porin purification techniques (insolubility in 2% sodium dodecyl sulfate, solubility in 0.4 M NaCl, and Sephacryl S-200 gel filtration), and then Synsorb H type 2 affinity chromatography was done. The physical and functional properties of the carbohydrate-reactive porins and CROMPs were found to be identical. On the basis of pore-forming properties in planar lipid bilayers and channel inhibition with maltotriose solutions, a nonspecific, general diffusion porin and a LamB-like maltoporin were identified in both CROMP and carbohydrate-reactive porin preparations. To our knowledge, the use of carbohydrate reactivity to isolate channel-forming proteins from bacterial outer membranes has not been reported previously. |
| Databáze: | OpenAIRE |
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