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rBPI 23 , a recombinant N-terminal fragment of human bactericidal/permeability-increasing protein (BPI), kills Gram-negative bacteria and neutralizes endotoxin. rBPI  21 , a variant in which cysteine 132 is changed to alanine, retains the activities of rBPI 23 . Analysis of certain purified rBPI  21  preparations revealed that some of the molecules had lost nine amino acids from the amino terminus. To explore the effect of this modification on structure and activity, we cloned and expressed a variant of rBPI  21 , designated rBPI(10-193), which lacks the first nine amino acids. A monoclonal antibody believed to recognize the amino terminus of rBPI  21  cross-reacted with rBPI 21 , but not with rBPI(10-193) or full length recombinant BPI (rBPI). These results demonstrated that the antibody recognizes the first nine amino acids of rBPI 21  and that this region of the holoprotein (rBPI) is inaccessible to the antibody (as suggested by the known 3-D structure). Purified rBPI(10193) and rBPI  21  were similarly potent in in vitro assays measuring bactericidal, endotoxin binding and neutralization activities. In a mouse model of lethal bacteremia, rBPI(10-193) and rBPI 21  were similarly potent whereas in a mouse endotoxin challenge model, rBPI(10-193) appeared to be at least 2-fold more potent than rBPI 21 . In conscious rats, a rapid bolus dose of 40 mg/kg of rBPI 21  caused a significant transient decrease in blood pressure while the same dose of rBPI(10-193) caused no blood pressure decrease. We conclude from these studies that the first nine amino acids of rBPI 21  are not essential for the anti-infective and endotoxin-neutralizing activities of BPI.

rBPI(10—193) is secreted by CHO cells and retains the activity of rBPI21