Characteristics of Novel Insect Defensin-Based Membrane-Disrupting Trypanocidal Peptides

Yamage, Mat; Yoshiyama, Mikio; Grab, Dennis J.; Kubo, Michinori; Iwasaki, Takashi; Kitani, Hiroshi; Ishibashi, Jun Ichiro; Yamakawa, Minoru

doi:10.1271/bbb.90004

Cited by 11 publications

(11 citation statements)

References 40 publications

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“…Incubation of T. brucei with melittin, a cytolytic peptide isolated from honey bee venom in submicromolar concentrations, resulted in a calcium influx into the parasites without disrupting cell permeability, which only occurs at higher concentrations (Ruben et al 1996). Our results also support other reports concerning the trypanocidal activity of several antimicrobially acting peptides of diverse origin which act by disrupting membrane integrity (Boulanger et al 2002;Kitani et al 2009;Löfgren et al 2008;McGwire et al 2003;Yamage et al 2009). …”

Section: Resultssupporting

confidence: 89%

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

et al. 2010

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Cupiennin 1a, a cytolytic peptide isolated from the venom of the spider Cupiennius salei, exhibits broad membranolytic activity towards bacteria, trypanosomes, and plasmodia, as well as human blood and cancer cells. In analysing the cytolytic activity of synthesised all-D-and all-L-cupiennin 1a towards pro-and eukaryotic cells, a stereospecific mode of membrane destruction could be excluded. The importance of negatively charged sialic acids on the outer leaflet of erythrocytes for the binding and haemolytic activity of L-cupiennin 1a was demonstrated. Reducing the overall negative charges of erythrocytes by partially removing their sialic acids or by protecting them with tri-or pentalysine results in reduced haemolytic activity of the peptide.

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Section: Resultssupporting

confidence: 89%

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

et al. 2010

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“…The role of AMPs in relation to C. bombi infection is unclear because their mechanism(s) of action remains poorly characterized (Boulanger et al, 2006). Although AMPs are potent antibacterial and antifungal peptides they do interact with and disrupt specific trypanosomes stages (Löfgren et al, 2008;Yamage et al, 2009) and reduce host susceptibility to trypanosome infection (Hu & Aksoy, 2006). The possibility remains that signalling occurs from the site of infection (ie gut) to immune tissues such as the fat body, to stimulate systemic expression of immune molecules such as the AMPs (Beschin et al, 2001;Boulanger et al, 2001;Foley, 2003).…”

Section: Late Response Genesmentioning

confidence: 99%

Pathways to immunity: temporal dynamics of the bumblebee (Bombus terrestris) immune response against a trypanosomal gut parasite

Riddell

Sumner²,

Adams

et al. 2011

Insect Molecular Biology

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Immune response dynamics in insects from natural host-parasite associations are poorly understood, despite accumulating evidence of ecological immune phenomena in these systems. Using a gene discovery approach, we have identified genes relating to signalling, enzymatic processes and respiration that were up-regulated in the bumblebee, Bombus terrestris, during infection with the trypanosomatid parasite, Crithidia bombi. In addition, we have mapped dynamic changes in the temporal expression of these genes and three candidate antimicrobial peptide (AMP) immune genes, Abaecin, Defensin and Hymenoptaecin, from 1 to 24 h after C. bombi infection. We show that dynamic changes in expression occur for individual genes at distinct phases of the immune response to C. bombi that correspond to early, intermediate and late stages of infection.

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“…The fungal ribotoxin protein α-sarcin has cytotoxic and anticancer properties that are thought to be mediated mainly through interaction with the plasma membrane, independently of receptors and endocytosis pathways. [1][2][3] As is well established, many pharmaceutically interesting peptides also work through perturbation of membrane integrity, [4][5][6][7][8] and these are under intense scrutiny for their cytotoxic action on cancer cells, as well as for their antibiotic properties. 6,[9][10][11][12] What both protein and peptide phenomena have in common is that they imply an affinity for membranes that is invariably enhanced by the presence of negatively charged bilayer components.…”

Section: Introductionmentioning

confidence: 99%

HAMLET Forms Annular Oligomers When Deposited with Phospholipid Monolayers

Baumann

Gjerde

Ying

et al. 2012

Journal of Molecular Biology

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Recently, the anticancer activity of human α-lactalbumin made lethal to tumor cells (HAMLET) has been linked to its increased membrane affinity in vitro, at neutral pH, and ability to cause leakage relative to the inactive native bovine α-lactalbumin (BLA) protein. In this study, atomic force microscopy resolved membrane distortions and annular oligomers (AOs) produced by HAMLET when deposited at neutral pH on mica together with a negatively charged lipid monolayer. BLA, BAMLET (HAMLET's bovine counterpart) and membrane-binding Peptide C, corresponding to BLA residues 75-100, also form AO-like structures under these conditions but at higher subphase concentrations than HAMLET. The N-terminal Peptide A, which binds to membranes at acidic but not at neutral pH, did not form AOs. This suggests a correlation between the capacity of the proteins/peptides to integrate into the membrane at neutral pH-as observed by liposome content leakage and circular dichroism experiments-and the formation of AOs, albeit at higher concentrations. Formation of AOs, which might be important to HAMLET's tumor toxic action, appears related to the increased tendency of the protein to populate intermediately folded states compared to the native protein, the formation of which is promoted by, but not uniquely dependent on, the oleic acid molecules associated with HAMLET.

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Characteristics of Novel Insect Defensin-Based Membrane-Disrupting Trypanocidal Peptides

Cited by 11 publications

References 40 publications

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

Pathways to immunity: temporal dynamics of the bumblebee (Bombus terrestris) immune response against a trypanosomal gut parasite

HAMLET Forms Annular Oligomers When Deposited with Phospholipid Monolayers

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