Hemolysin

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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]] }}
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== 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 ==
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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

Template:STRUCTURE 7ahl

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

  1. 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
  2. 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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Michal Harel, Mark Hoelzer, Wayne Decatur, Alexander Berchansky

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