Histidine-rich glycoprotein exerts antibacterial activity.
(2007) In The FEBS Journal 274(2). p.377-389- Abstract
- 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. faecalisbacteria in the presence of Zn2+ 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... (More)
- 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. faecalisbacteria in the presence of Zn2+ 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 Zn2+ 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/164825
- author
- Rydengård, Victoria LU ; Olsson, Anna-Karin ; Mörgelin, Matthias LU and Schmidtchen, Artur LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The FEBS Journal
- volume
- 274
- issue
- 2
- pages
- 377 - 389
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000243234500010
- scopus:33845970531
- ISSN
- 1742-464X
- DOI
- 10.1111/j.1742-4658.2006.05586.x
- language
- English
- LU publication?
- yes
- id
- 5eb78332-ae2f-41d6-ae52-ff8554120a32 (old id 164825)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17229145&dopt=Abstract
- date added to LUP
- 2016-04-01 16:39:27
- date last changed
- 2022-03-07 07:26:04
@article{5eb78332-ae2f-41d6-ae52-ff8554120a32, abstract = {{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. faecalisbacteria in the presence of Zn2+ 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 Zn2+ 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.}}, author = {{Rydengård, Victoria and Olsson, Anna-Karin and Mörgelin, Matthias and Schmidtchen, Artur}}, issn = {{1742-464X}}, language = {{eng}}, number = {{2}}, pages = {{377--389}}, publisher = {{Wiley-Blackwell}}, series = {{The FEBS Journal}}, title = {{Histidine-rich glycoprotein exerts antibacterial activity.}}, url = {{https://lup.lub.lu.se/search/files/4737465/625847.pdf}}, doi = {{10.1111/j.1742-4658.2006.05586.x}}, volume = {{274}}, year = {{2007}}, }