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Role of the bactericidal/permeability-increasing protein in host defence

Open access
Elsbach, Peter, Weiss, Jerrold·1998·Current Opinion in Immunology

Abstract

Much has been learned recently about the structure and function of 55 kDa bactericidal/permeability-increasing protein (BPI), a member of a genomically conserved lipid-interactive protein family. Analysis of BPI fragments and the crystal structure of human BPI have established that BPI consists of two functionally distinct domains: a potently antibacterial and anti-endotoxin amino-terminal domain (approximately 20 kDa) and a carboxy-terminal portion that imparts opsonic activity to BPI. A recombinant amino-terminal fragment (rBPI21) protects animals against the effects of Gram-negative bacteria and endotoxin. In man, rBPI21 is nontoxic and non-immunogenic and is in Phase II/III clinical trials with apparent therapeutic benefit.

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Metadata

Authors
Elsbach, P., & Weiss, J.
Venue
Current Opinion in Immunology
Publisher
Elsevier BV
Published
1998-02
Volume
10
Issue
1
Pages
45-49
ISSN
0952-7915 (ISSN-L)
OpenAlex
W2064768582
Cited by
214
References
0
FWCI
0.71
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Role of the bactericidal/permeability-increasing protein in host defence. https://app.cochat.ai/papers/10.1016/s0952-7915(98)80030-7
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Elsbach, P., & Weiss, J. (1998). Role of the bactericidal/permeability-increasing protein in host defence. Current Opinion in Immunology. https://doi.org/10.1016/s0952-7915(98)80030-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.