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. 2010 Aug 12;6(8):e1001047. doi: 10.1371/journal.ppat.1001047

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Phage lysin is exported through the holin pore and mounted on the bacterial surface of the same or adjacent organisms through its interaction with PC residues. Lysin can then mediate platelet binding via its interaction with fibrinogen and glycoprotein IIb/IIIa (GPIIb/IIIa), which is the principal fibrinogen receptor on platelets. Through its amidase activity, lysin can also permeabilize the cell wall, permitting the release and surface expression PblA and PblB. These phage proteins also interact with platelets by binding the membrane ganglioside GD3.