Disease relevance of BPI

• Binding of PmB, BPI, LALF, or anti-DCLA mAb 1B6 to Salmonella minnesota monophosphoryl lipid A (MPLA), diphosphoryl lipid A (DPLA), and Salmonella minnesota Re (which possess a common structural moiety, but vary considerably in structure and charge) was examined [1].

High impact information on BPI

• Nucleotide sequence of the bovine bactericidal permeability increasing protein (BPI) [2].
• Binding specificity of polymyxin B, BPI, LALF, and anti-deep core/lipid a monoclonal antibody to lipopolysaccharide partial structures [1].
• Bactericidal/permeability-increasing protein (BPI) was originally identified as a lipopolysaccharide (LPS) binding protein with gram-negative bactericidal activity in the leukocytes [3].

Associations of BPI with chemical compounds

• BPI bound MPLA, which is hydrophobic and minimally charged, while mAb 1B6 bound anionic DNA; neither PmB nor LALF were reactive with MPLA or DNA [1].

References