Recombinant Escherichia coli Lipopolysaccharide assembly protein B (lapB), partial

Amino acids 17-389 form the expressed segment for recombinant Escherichia coli (strain K12) lapB. This lapB protein is theoretically predicted to have a molecular weight of 58.8 kDa. This lapB protein is produced using e.coli expression system. The N-terminal 6xHis-SUMO tag was smoothly integrated into the coding gene of lapB, which enables a simple process of detecting and purifying the lapB recombinant protein in the following steps.

Lipopolysaccharide assembly protein B (LapB) in Escherichia coli plays a crucial role in the assembly and transport of lipopolysaccharide (LPS), a major component of the bacterial outer membrane. LPS is essential for maintaining the integrity and permeability of the outer membrane, as well as serving as a key virulence factor. LapB is involved in the coordination of LPS biosynthesis and its transport to the outer membrane. It interacts with components of the LPS transport machinery, facilitating the efficient incorporation of newly synthesized LPS into the growing outer membrane. The proper functioning of LapB is essential for the formation of a protective barrier against environmental stresses and host immune responses. Understanding the role of LapB contributes to insights into bacterial membrane biogenesis, outer membrane integrity, and the potential development of strategies to disrupt bacterial virulence and survival mechanisms.