Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations

P. W. Gray, G. Flaggs, S. R. Leong, Richard J Gumina, J. Weiss, C. E. Ooi, P. Elsbach

Research output: Contribution to journalArticle

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Abstract

The bactericidal permeability increasing protein (BPI) is a 50-60-kDa membrane-associated protein isolated from granules of polymorphonuclear leukocytes. A full-length cDNA clone encoding human BPI has been isolated and the derived amino acid sequence reveals a structure that is consistent with previously determined biological properties. BPI may be organized into two domains: the amino-terminal half, previously shown to contain all known antimicrobial activity, contains a large fraction of basic and hydrophilic residues. In contrast, the carboxyl-terminal half contains more acidic than basic residues and includes several potential transmembrane regions which may anchor the holoprotein in the granule membrane. The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic amino-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial envelope. The amino-terminal end of BPI exhibits significant similarity with the sequence of a rabbit lipopolysaccharide-binding protein, suggesting that both molecules share a similar structure for binding lipopolysaccharides.

Original languageEnglish (US)
Pages (from-to)9505-9509
Number of pages5
JournalJournal of Biological Chemistry
Volume264
Issue number16
StatePublished - Jan 1 1989

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Cloning
Organism Cloning
Neutrophils
Complementary DNA
Proteins
Lipopolysaccharides
Anchors
Gram-Negative Bacteria
Membrane Potentials
Amino Acid Sequence
Bacteria
Membrane Proteins
Clone Cells
bactericidal permeability increasing protein
Rabbits
Membranes
Amino Acids
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Gray, P. W., Flaggs, G., Leong, S. R., Gumina, R. J., Weiss, J., Ooi, C. E., & Elsbach, P. (1989). Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations. Journal of Biological Chemistry, 264(16), 9505-9509.

Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations. / Gray, P. W.; Flaggs, G.; Leong, S. R.; Gumina, Richard J; Weiss, J.; Ooi, C. E.; Elsbach, P.

In: Journal of Biological Chemistry, Vol. 264, No. 16, 01.01.1989, p. 9505-9509.

Research output: Contribution to journalArticle

Gray, PW, Flaggs, G, Leong, SR, Gumina, RJ, Weiss, J, Ooi, CE & Elsbach, P 1989, 'Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations', Journal of Biological Chemistry, vol. 264, no. 16, pp. 9505-9509.
Gray PW, Flaggs G, Leong SR, Gumina RJ, Weiss J, Ooi CE et al. Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations. Journal of Biological Chemistry. 1989 Jan 1;264(16):9505-9509.
Gray, P. W. ; Flaggs, G. ; Leong, S. R. ; Gumina, Richard J ; Weiss, J. ; Ooi, C. E. ; Elsbach, P. / Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations. In: Journal of Biological Chemistry. 1989 ; Vol. 264, No. 16. pp. 9505-9509.
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