Authored: Jupe, S, 2011-04-28 Reviewed: McDermott, AM, 2011-11-03 In S. aureus, rather than cause gross membrane changes, HNP-1 (de Leeuw et al. 2010) and hBD3 (Sass et al. 2011) appear to interfere with cell wall biosynthetic pathways by binding to Lipid II (undecaprenylpyrophosphate-MurNAc[pentapeptide]-GlcNAc), an essential precursor of bacterial cell walls and the target of several antibiotics (Breukink & de Krujiff 2007). The transformation of monomeric lipid II into a polymeric peptidoglycan by the bifunctional S. aureus enzyme Penicillin-binding protein 2 (PBP2) is inhibited by hBD3 (Sass et al. 2011) resulting in local lesions of the cell wall layer through which membranes and cytoplasmic contents ultimately protrude. Edited: Jupe, S, 2011-07-27

http://purl.obolibrary.org/obo/HINO_0008035

Authored: Jupe, S, 2011-04-28

Reviewed: McDermott, AM, 2011-11-03

In S. aureus, rather than cause gross membrane changes, HNP-1 (de Leeuw et al. 2010) and hBD3 (Sass et al. 2011) appear to interfere with cell wall biosynthetic pathways by binding to Lipid II (undecaprenylpyrophosphate-MurNAc[pentapeptide]-GlcNAc), an essential precursor of bacterial cell walls and the target of several antibiotics (Breukink & de Krujiff 2007). The transformation of monomeric lipid II into a polymeric peptidoglycan by the bifunctional S. aureus enzyme Penicillin-binding protein 2 (PBP2) is inhibited by hBD3 (Sass et al. 2011) resulting in local lesions of the cell wall layer through which membranes and cytoplasmic contents ultimately protrude.

Edited: Jupe, S, 2011-07-27

Pubmed20214904

Reactome, http://www.reactome.org

Pubmed16531990

Pubmed20385753

http://purl.obolibrary.org/obo/HINO_0008359

http://purl.obolibrary.org/obo/CHEBI_27692

http://purl.obolibrary.org/obo/HINO_0003199

Binding of defensins to lipid II

HINO:0008035

Binding of defensins to lipid II

Reactome Database ID Release 431467209

ReactomeREACT_115839

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