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Studies on the interactions of neutral Galleria mellonella cecropin D with living bacterial cells

Overview of attention for article published in Amino Acids, August 2018
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Title
Studies on the interactions of neutral Galleria mellonella cecropin D with living bacterial cells
Published in
Amino Acids, August 2018
DOI 10.1007/s00726-018-2641-4
Pubmed ID
Authors

Agnieszka Zdybicka-Barabas, Sylwia Stączek, Bożena Pawlikowska-Pawlęga, Paweł Mak, Rafał Luchowski, Krzysztof Skrzypiec, Ewaryst Mendyk, Jerzy Wydrych, Wiesław I. Gruszecki, Małgorzata Cytryńska

Abstract

Cecropins constitute an important family of insect antimicrobial peptides involved in humoral innate immune response. In comparison with the highly basic cecropins A and B, cecropins D are less cationic and more hydrophobic. Interestingly, cecropins D were described only in lepidopteran insects, e.g., the greater wax moth Galleria mellonella. In the present study, interactions of neutral cecropin D (pI 6.47) purified from hemolymph of G. mellonella with living Escherichia coli cells were investigated. Fluorescence lifetime imaging microscopy using fluorescein isothiocyanate-labeled cecropin D revealed very fast binding of the peptide to E. coli cells. Fourier transform infrared spectroscopy analyses showed that G. mellonella cecropin D interacted especially with E. coli LPS and probably other lipid components of the bacterial cell envelope and exhibited an ordering effect with regard to lipid chains. This effect is consistent with the peptide binding mechanism based upon its incorporation into the lipid phase of the cell membrane. The interaction resulted in permeabilization of the bacterial cell membrane. Upon cecropin D binding, the cells lost characteristic surface topography, which was accompanied by altered nanomechanical properties, as revealed by atomic force microscopy. The interaction of the peptide with the bacterial cells also led to intracellular damage, i.e., loss of the cell envelope multilayer structure, formation of membrane vesicles, and enlargement of periplasmic space, which eventually caused death of the bacteria. In summary, it can be concluded that amphipathic character of α-helices, exposure of small positively charged patches on their polar surfaces and hydrophobic interactions are important physicochemical characteristics related to effective binding to E. coli cells and antibacterial activity of neutral G. mellonella cecropin D.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 8 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 4 50%
Unspecified 3 38%
Student > Master 1 13%
Readers by discipline Count As %
Unspecified 4 50%
Biochemistry, Genetics and Molecular Biology 2 25%
Immunology and Microbiology 2 25%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 01 September 2018.
All research outputs
#11,929,783
of 13,454,271 outputs
Outputs from Amino Acids
#886
of 1,057 outputs
Outputs of similar age
#229,270
of 266,085 outputs
Outputs of similar age from Amino Acids
#15
of 17 outputs
Altmetric has tracked 13,454,271 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,057 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 6.0. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 266,085 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 17 others from the same source and published within six weeks on either side of this one. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.