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Cited by 370

The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.

Interaction between Heat Shock Proteins and Antimicrobial Peptides

Otvos,, Laszlo, O, Insug, Rogers, Mark E., Consolvo, Patricia J., Condie, Barry A., Lovas, Sandor, Bulet, Philippe, Blaszczyk-Thurin, Magdalena·2000·Biochemistry
DOI 10.1021/bi0012843
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Abstract

Drosocin, pyrrhocoricin, and apidaecin, representing the short (18-20 amino acid residues) proline-rich antibacterial peptide family, originally isolated from insects, were shown to act on a target bacterial protein in a stereospecific manner. Native pyrrhocoricin and one of its analogues designed for this purpose protect mice from bacterial challenge and, therefore, may represent alternatives to existing antimicrobial drugs. Furthermore, this mode of action can be a basis for the design of a completely novel set of antibacterial compounds, peptidic or peptidomimetic, if the interacting bacterial biopolymers are known. Recently, apidaecin was shown to enter Escherichia coli and subsequently kill bacteria through sequential interactions with diverse target macromolecules. In this paper report, we used biotin- and fluorescein-labeled pyrrhocoricin, drosocin, and apidaecin analogues to identify biopolymers that bind to these peptides and are potentially involved in the above-mentioned multistep killing process. Through use of a biotin-labeled pyrrhocoricin analogue, we isolated two interacting proteins from E. coli. According to mass spectrometry, Western blot, and fluorescence polarization, the short, proline-rich peptides bound to DnaK, the 70-kDa bacterial heat shock protein, both in solution and on the solid-phase. GroEL, the 60-kDa chaperonin, also bound in solution. Control experiments with an unrelated labeled peptide showed that while binding to DnaK was specific for the antibacterial peptides, binding to GroEL was not specific for these insect sequences. The killing of bacteria and DnaK binding are related events, as an inactive pyrrhocoricin analogue made of all-D-amino acids failed to bind. The pharmaceutical potential of the insect antibacterial peptides is underscored by the fact that pyrrhocoricin did not bind to Hsp70, the human equivalent of DnaK. Competition assay with unlabeled pyrrhocoricin indicated differences in GroEL and DnaK binding and a probable two-site interaction with DnaK. In addition, all three antibacterial peptides strongly interacted with two bacterial lipopolysaccharide (LPS) preparations in solution, indicating that the initial step of the bacterial killing cascade proceeds through LPS-mediated cell entry.

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Metadata

Authors
Otvos, O, I., Rogers, M. E., Consolvo, P. J., Condie, B. A., Lovas, S., Bulet, P., & Blaszczyk-Thurin, M.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2000-10-21
Volume
39
Issue
46
Pages
14150-14159
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi0012843
OpenAlex
W1995412010
Cited by
370
References
17
FWCI
5.73
Type
journal article
Language
en
Open access
closed

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