Hemolysin
From Proteopedia
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{{STRUCTURE_7ahl|  PDB=7ahl  | SIZE=400| SCENE= |right|CAPTION=α-hemolysin heptamer, [[7ahl]] }}  | {{STRUCTURE_7ahl|  PDB=7ahl  | SIZE=400| SCENE= |right|CAPTION=α-hemolysin heptamer, [[7ahl]] }}  | ||
| - | + | == Function ==  | |
'''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells<ref>PMID:20110774</ref>. Hemolysin from the bacterium ''Clostridium'' are called '''alpha-toxin''' (AT).  AT is a zinc metalloenzyme and binds to the membrane in the presence of calcium. It acts as a phospholipase C.    | '''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells<ref>PMID:20110774</ref>. Hemolysin from the bacterium ''Clostridium'' are called '''alpha-toxin''' (AT).  AT is a zinc metalloenzyme and binds to the membrane in the presence of calcium. It acts as a phospholipase C.    | ||
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For toxins in Proteopdia see [[Toxins]].  | For toxins in Proteopdia see [[Toxins]].  | ||
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| + | == Relevance ==  | ||
| + | HL acts as a virulence factor in the pathogenesis of invasive infections<ref>PMID:12564994</ref>.  | ||
== 3D Structures of hemolysin ==  | == 3D Structures of hemolysin ==  | ||
Revision as of 08:01, 21 March 2016
Contents | 
Function
Hemolysin (HL) is exotoxin from bacteria which causes lysis of red blood cells[1]. Hemolysin from the bacterium Clostridium are called alpha-toxin (AT). AT is a zinc metalloenzyme and binds to the membrane in the presence of calcium. It acts as a phospholipase C.
See details for α-hemolysin in Pore forming toxin, α-hemolysin. See details of hemolysin E in Molecular Playground/ClyA.
For toxins in Proteopdia see Toxins.
Relevance
HL acts as a virulence factor in the pathogenesis of invasive infections[2].
3D Structures of hemolysin
Updated on 21-March-2016
A full page in Proteopedia exploring 7ahl is found here.
References
- ↑ Mestre MB, Fader CM, Sola C, Colombo MI. Alpha-hemolysin is required for the activation of the autophagic pathway in Staphylococcus aureus-infected cells. Autophagy. 2010 Jan;6(1):110-25. PMID:20110774
 - ↑ Nizet V. Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 2002 Dec;10(12):575-80. PMID:12564994
 
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