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Lipopolysaccharide (LPS) is a major constituent of the outer membrane of Gram-negative bacteria and acts as a pathogen-associated molecular pattern that triggers immune responses in both plants and animals. LPS-binding protein (LBP) and bactericidal/permeability-increasing protein (BPI), which bind to LPS and play important roles in immunity of mammals, have been well studied. However, the molecule contributing to LPS binding in plants is mostly unknown. The  Arabidopsis  genome carries two genes encoding LBP/BPI-related proteins which we designated as  AtLBP/BPI related-1  ( AtLBR-1 ) and  AtLBP/BPI related-2  ( AtLBR-2 ). We found that their N-terminal domains were co-purified with cell wall-derived LPS when expressed in  E. coli . Since this finding implied the direct binding of AtLBRs to LPS, we also confirmed binding by using LPS-free AtLBRs and purified LPS. AtLBRs directly bind to both rough and smooth types of LPS. We also demonstrated that LPS-treated  atlbr  mutant  Arabidopsis  exhibit a significant delay of induction of defence-related gene  pathogenesis-related 1  ( PR1 ) but no other  PR  genes. Furthermore, LPS-treated  atlbr  mutants showed defects in reactive oxygen species (ROS) generation. These results demonstrate that, as well as LBP and BPI of mammals, AtLBRs also play an important role in the LPS-induced immune response of plants.

Arabidopsis LBP/BPI related-1 and -2 bind to LPS directly and regulate PR1 expression