Bacterial Lipoproteins - So many with the same modification

Covalent modification of a protein with lipid was first identified in 1969 in the major outer membrane protein of E.coli. The structure (N-acylS-diacylglyceryl Cysteine at the N-terminal) of the lipid was elucidated by Braun in 1973 and therefore it is called Braun's lipoprotein [1]. Subsequently more than 400 proteins with the same modification have been identified in all known bacteria. These lipoproteins are either structural proteins or enzymes or receptors or transporters performing essential functions at the membrane-aqueous interface [2]. There are more than 275 distinct lipoproteins as can be seen in the table. The lipoproteins have been grouped according to their functional nature.

Classification of Bacterial Lipoproteins

• Structural Proteins
• Adhesins
• Antigens
• Enzymes
• Transporters
• Binding Proteins
• Toxins
• Interesting Factors
• Hypothetical Lipoproteins

References

1) Braun, V. and Rehn, K., Chemical characterization, spatial distribution, and function of a lipoprotein (murein-lipoprotein) of the E.coli cell wall, Eur.J.Biochem., 10, 426, 1969.

2)Hantke, K. and Braun, V., Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murien -lipoprotein of the Eschericia coli outer membrane, Eur. J. Biochem., 34, 284, 1973.

3) Braun, V., and H. C. Wu. 1993. Lipoproteins, structure, function, biosynthesis and model for protein export, p. 319 - 342. In J-M Ghuysen and R. Hakenback (ed), Comprehensive biochemistry, vol 27. Bacterial cell wall. Elsevier Science Publishers, B.V.Amsterdam.

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