Disease relevance of lamB

• Combinatorial mutagenesis of the lamB gene: residues 41 through 43, which are conserved in Escherichia coli outer membrane proteins, are informationally important in maltoporin structure and function [1].
• To validate this notion in nonenteric bacteria, the expression and correct processing of LamB were confirmed by coupling the lamB gene to the salicylate-responsive Psa1 promoter of the NAH7 (naphthalene degradation) plasmid in Pseudomonas putida [2].
• Plasmid pBCP 68 carrying the lamB gene of Escherichia coli was introduced and expressed in Yersinia enterocolitica cells [3].
• Molecular cloning and nucleotide sequence analysis of the maltose-inducible porin gene of Aeromonas salmonicida [4].

High impact information on lamB

• This fusion did not map in any of the known genes of the malA or malB region, but its expression was under control of malT, the positive regulator gene of the maltose regulon [5].
• The cloned 2.2-kb Sau3AI DNA fragment from F. mortiferum contained a second partial open reading frame of 83 residues (designated malB) that was located immediately upstream of malH [6].
• A new suppressor of a lamB signal sequence mutation, prlZ1, maps to 69 minutes on the Escherichia coli chromosome [7].
• Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch polysaccharides [8].
• Base up-regulated core genes for maltodextrin transport (lamB, mal), ATP synthase (atp), and DNA repair (recA, mutL) [9].

Associations of lamB with chemical compounds

• In contrast to maltose transport in untreated cells, that of Ca++-treated lamB cells was inhibited by anti-MBP (maltose-binding protein) antibodies [10].

References