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An invading pathogen must be held in check by the innate immune system until a specific immune response can be mounted. In the case of Gram-negative bacteria, the principal stimulator is LPS, a component of the outer membrane of the bacteria. In vitro LPS is bound by LBP and transferred to the LPS receptor CD14 on the macrophage surface. Binding to CD14 triggers an inflammatory response which is crucial for keeping an infection under control. In vitro, LBP mediates a response not only to LPS but also to intact Gram-negative bacteria. We show that whole Escherichia coli bacteria are recognised by CD14 on human monocytes, and subsequently may become phagocytosed. Although neither LBP nor CD14 interact with the heat inactivated, intact Gram-positive bacterium Bacillus subtilis both proteins form stable complexes with lipoteichoic acid derived from the bacterial cell wall. A brief exposure of B. subtilis to serum or antibiotics converts them into a form which can be recognised by CD14 in an LBP-dependent manner followed by phagocytosis. In preliminary experiments, it is shown that LBP is essential in vitro for the oxidative burst response of mouse macrophages induced by living Salmonella typhimurium as well as Staphylococcus epidermidis. Our results indicate that, in addition to CD14, LBP is also a pattern recognition element and is required to induce a rapid inflammatory response to Gram-negative as well as to Gram-positive bacteria and to initiate their phagocytosis. [ABSTRACT FROM PUBLISHER]

HLA‐C*14:93 N differs from 14:02:01 by a single nucleotide substitution at position 502 in Exon 3. [ABSTRACT FROM AUTHOR]

HLA‐B*50:01:09 differs by a synonymous nucleotide exchange in codon 17 from B*50:01:01. [ABSTRACT FROM AUTHOR]

HLA‐C*03:376 differs from HLA‐C*03:04:01 in exon 6 by a single nucleotide substitution. [ABSTRACT FROM AUTHOR]

HLA‐C*04:01:85 differs in exon 1 from C*04:01:01 by a single nucleotide substitution in codon 3. [ABSTRACT FROM AUTHOR]