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Histidine‐rich glycoprotein exerts antibacterial activity
Author(s) -
Rydengård Victoria,
Olsson AnnaKarin,
Mörgelin Matthias,
Schmidtchen Artur
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05586.x
Subject(s) - antibacterial activity , heparin , histidine , biochemistry , enterococcus faecalis , bacteria , biology , pseudomonas aeruginosa , microbiology and biotechnology , chemistry , escherichia coli , enzyme , genetics , gene
Histidine‐rich glycoprotein (HRGP), an abundant heparin‐binding protein found in plasma and thrombocytes, exerts antibacterial effects against Gram‐positive bacteria ( Enterococcus faecalis and Staphylococcus aureus ) and Gram‐negative bacteria ( Escherichia coli and Pseudomonas aeruginosa ). Fluorescence studies and electron microscopy to assess membrane permeation showed that HRGP induces lysis of E. faecalis bacteria in the presence of Zn 2+ or at low pH. Heparin blocked binding of the protein to E. faecalis and abolished antibacterial activity. Furthermore, truncated HRGP, devoid of the heparin‐binding and histidine‐rich domain, was not antibacterial. It has previously been shown that peptides containing consensus heparin‐binding sequences (Cardin and Weintraub motifs) are antibacterial. Thus, the peptide (GHHPH) 4 , derived from the histidine‐rich region of HRGP and containing such a heparin‐binding motif, was antibacterial for E. faecalis in the presence of Zn 2+ or at low pH. The results show a previously undisclosed antibacterial activity of HRGP and suggest that the histidine‐rich and heparin‐binding domain of HRGP mediates the antibacterial activity of the protein.