1s6w
From Proteopedia
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[[Image:1s6w.gif|left|200px]] | [[Image:1s6w.gif|left|200px]] | ||
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'''Solution Structure of hybrid white striped bass hepcidin''' | '''Solution Structure of hybrid white striped bass hepcidin''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S6W is a [[Single protein]] structure | + | 1S6W is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Singh, S.]] | [[Category: Singh, S.]] | ||
[[Category: Westerman, M E.]] | [[Category: Westerman, M E.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:22:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:22, 3 May 2008
Solution Structure of hybrid white striped bass hepcidin
Overview
Bass hepcidin was purified from the gill of hybrid striped bass (Morone chrysops x Morone saxatilis) based on antimicrobial activity against Escherichia coli. This 21-amino acid peptide has 8 cysteines engaged in 4 disulfide bonds and is very similar to human hepcidin, an antimicrobial peptide with iron regulatory properties. To gain insight into potential role(s) of bass hepcidin in innate immunity in fish, we synthesized the peptide, characterized its antimicrobial activities in vitro, determined its solution structure by NMR, and quantified hepatic gene expression in vivo following infection of bass with the fish pathogens, Streptococcus iniae or Aeromonas salmonicida. Its structure is very similar to that of human hepcidin, including the presence of an antiparallel beta-sheet, a conserved disulfide-bonding pattern, and a rare vicinal disulfide bond. Synthetic bass hepcidin was active in vitro against Gram-negative pathogens and fungi but showed no activity against key Gram-positive pathogens and a single yeast strain tested. Hepcidin was non-hemolytic at microbicidal concentrations and had lower specific activity than moronecidin, a broad spectrum, amphipathic, alpha-helical, antimicrobial peptide constitutively expressed in bass gill tissue. Good synergism between the bacterial killing activities of hepcidin and moronecidin was observed in vitro. Hepcidin gene expression in bass liver increased significantly within hours of infection with Gram-positive (S. iniae) or Gram-negative (A. salmonicida) pathogens and was 4-5 orders of magnitude above base-line 24-48 h post-infection. Our results suggest that hepcidin plays a key role in the antimicrobial defenses of bass and that its functions are potentially conserved between fish and human.
About this Structure
1S6W is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Bass hepcidin synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections., Lauth X, Babon JJ, Stannard JA, Singh S, Nizet V, Carlberg JM, Ostland VE, Pennington MW, Norton RS, Westerman ME, J Biol Chem. 2005 Mar 11;280(10):9272-82. Epub 2004 Nov 16. PMID:15546886 Page seeded by OCA on Sat May 3 08:22:23 2008
