Human Interaction Network Ontology

Last uploaded: June 27, 2014
Preferred Name

Beta-defensins bind microbial membranes causing disruption
Synonyms
Definitions

Authored: Jupe, S, 2011-04-28 Reviewed: McDermott, AM, 2011-11-03 Edited: Jupe, S, 2011-07-27 Binding and disruption of microbial membranes is widely believed to be the primary mechanism of action for beta-defensins. There is no direct evidence of this, but a growing number of studies support this model (Pazgier et al. 2006). Beta-defensins have antimicrobial properties that correlate with membrane permeabilization effects (Antcheva et al. 2004, Sahl et al. 2005, Yenugu et al. 2004). The sensitivity of microbes to beta-defensins correlates with the lipid composition of the membrane; more negatively-charged lipids correlate with larger beta-defensin 103-induced changes in membrane capacitance (Bohling et al. 2006). Beta-defensin-103 was observed to give rise to ionic currents in Xenopus membranes (Garcia et al. 2001) and cell wall perforation was observed in S. aureus when treated with HBD-3 (Harder et al. 2001). Two models explain how membrane disruption takes place. The 'pore model' postulates that beta-defenisns form transmembrane pores in a similar manner to alpha-defensins, while the 'carpet model' suggests that beta-defensins act as detergents, causing a less organised disruption. Beta-defensins have a structure that is topologically distinct from that of alpha-defensins, suggesting a different mode of dimerization and an electrostatic charge-based mechanism of membrane permeabilization rather than a mechanism based on formation of bilayer-spanning pores (Hoover et al. 2000).

ID

http://purl.obolibrary.org/obo/HINO_0008030

comment

Authored: Jupe, S, 2011-04-28

Reviewed: McDermott, AM, 2011-11-03

Edited: Jupe, S, 2011-07-27

Binding and disruption of microbial membranes is widely believed to be the primary mechanism of action for beta-defensins. There is no direct evidence of this, but a growing number of studies support this model (Pazgier et al. 2006). Beta-defensins have antimicrobial properties that correlate with membrane permeabilization effects (Antcheva et al. 2004, Sahl et al. 2005, Yenugu et al. 2004). The sensitivity of microbes to beta-defensins correlates with the lipid composition of the membrane; more negatively-charged lipids correlate with larger beta-defensin 103-induced changes in membrane capacitance (Bohling et al. 2006). Beta-defensin-103 was observed to give rise to ionic currents in Xenopus membranes (Garcia et al. 2001) and cell wall perforation was observed in S. aureus when treated with HBD-3 (Harder et al. 2001). Two models explain how membrane disruption takes place. The 'pore model' postulates that beta-defenisns form transmembrane pores in a similar manner to alpha-defensins, while the 'carpet model' suggests that beta-defensins act as detergents, causing a less organised disruption. Beta-defensins have a structure that is topologically distinct from that of alpha-defensins, suggesting a different mode of dimerization and an electrostatic charge-based mechanism of membrane permeabilization rather than a mechanism based on formation of bilayer-spanning pores (Hoover et al. 2000).

definition source

Pubmed15582982

Reactome, http://www.reactome.org

Pubmed11702237

Pubmed10906336

Pubmed16634647

Pubmed14742239

Pubmed15033915

Pubmed11085990

Pubmed16710608

has input

http://purl.obolibrary.org/obo/CHEBI_62643

http://purl.obolibrary.org/obo/HINO_0008284

has output

http://purl.obolibrary.org/obo/HINO_0003205

label

Beta-defensins bind microbial membranes causing disruption

prefixIRI

HINO:0008030

prefLabel

Beta-defensins bind microbial membranes causing disruption

seeAlso

Reactome Database ID Release 431467269

ReactomeREACT_115564

subClassOf

http://purl.obolibrary.org/obo/INO_0000040

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